GlycoNAVI Proteins

GlycoNAVI-Proteins is dataset of glycan and protein information. This is the content of GlycoNAVI.

Source Last Updated
GlycoNAVI Proteins November 21, 2024
Displaying entries 3301 - 3350 of 39437 in total
PDB ID UniProt ID Title Descriptor ▼
2Q9O Q70KY3 Near-atomic resolution structure of a Melanocarpus albomyces laccase Laccase-1 (E.C.1.10.3.2)
3FU8 Q70KY3 Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol Laccase-1 (E.C.1.10.3.2)
3FU9 Q70KY3 Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol Laccase-1 (E.C.1.10.3.2)
5MHV I1VE66 The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The fourth structure of the series with total exposition time 93 min. Laccase 2 (E.C.1.10.3.2)
5EHF 5EHF Laccase from Antrodiella faginea Laccase (E.C.1.10.3.2)
3PPS 3PPS Crystal structure of an ascomycete fungal laccase from Thielavia arenaria Laccase
1LZS P00695 STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0 LYSOZYME (LZ604) (E.C.3.2.1.17) COMPLEXED WITH N-ACETYLCHITOSE OLIGOMERS
1LZR P00695 STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0 LYSOZYME (LZ406) (E.C.3.2.1.17) COMPLEXED WITH TETRA-ACETYL-CHITOTETRAOSE
1LZE P00698 DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY LYSOZYME (E.C.3.2.1.17) MUTANT WITH TRP 62 REPLACED BY TYR (W62Y) CO-CRYSTALLIZED WITH TRI-N-ACETYL-CHITOTRIOSE (PH 4.7)
1LZG P00698 DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY LYSOZYME (E.C.3.2.1.17) MUTANT WITH TRP 62 REPLACED BY PHE (W62F) CO-CRYSTALLIZED WITH TRI-N-ACETYL-CHITOTRIOSE (PH 4.7)
1LSZ P00698 CRYSTAL STRUCTURE OF THE MUTANT D52S HEN EGG WHITE LYSOZYME WITH AN OLIGOSACCHARIDE PRODUCT LYSOZYME (E.C.3.2.1.17) MUTANT WITH ASP 52 REPLACED BY SER (D52S) COMPLEXED WITH GLCNAC4 (TETRA-N-ACETYL CHITOTETRAOSE)
1HEW P00698 REFINEMENT OF AN ENZYME COMPLEX WITH INHIBITOR BOUND AT PARTIAL OCCUPANCY. HEN EGG-WHITE LYSOZYME AND TRI-N-ACETYLCHITOTRIOSE AT 1.75 ANGSTROMS RESOLUTION LYSOZYME (E.C.3.2.1.17) COMPLEXED WITH THE INHIBITOR TRI-N-ACETYLCHITOTRIOSE
1LZB P00698 DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY LYSOZYME (E.C.3.2.1.17) CO-CRYSTALLIZED WITH TRI-N-ACETYL-CHITOTRIOSE (PH 4.7)
1LZC P00698 DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY LYSOZYME (E.C.3.2.1.17) CO-CRYSTALLIZED WITH TETRA-N-ACETYL-CHITOTETRAOSE (PH 4.7)
1LMT P00695 STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME LYSOZYME (E.C.3.2.1.17) (LZ_CRGD4) MUTANT WITH CYS-ARG-GLY-ASP-SER-CYS INSERTED BETWEEN VAL 74 AND ASN 75 (INS(74-CRFDSC-75) COMPLEXED WITH TRI-ACETYL-CHITOTRIOSE
154L P00718 THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE LYSOZYME (E.C.3.2.1.17)
1LZY P00703 X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM LYSOZYME (E.C.3.2.1.17)
1SF4 P00698 BINDING OF N,N'-DIACETYLCHITOBIOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY LYSOZYME (E.C.3.2.1.17)
1SF6 P00698 BINDING OF N,N',N"-TRIACETYLCHITOTRIOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY LYSOZYME (E.C.3.2.1.17)
1SF7 P00698 BINDING OF TETRA-N-ACETYLCHITOTETRAOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY LYSOZYME (E.C.3.2.1.17)
1SFB P00698 BINDING OF PENTA-N-ACETYLCHITOPENTAOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY LYSOZYME (E.C.3.2.1.17)
1SFG P00698 BINDING OF HEXA-N-ACETYLCHITOHEXAOSE: A POWDER DIFFRACTION STUDY LYSOZYME (E.C.3.2.1.17)
4AKM Q9UQV4 Crystal structure of the human lysosome-associated membrane protein LAMP-3 (aka DC-LAMP) LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN 3
4US5 W8QCH3 Crystal Structure of apo-MsnO8 LUCIFERASE-LIKE MONOOXYGENASE
3CAY 3CAY Crystal structure of Lipopeptide Detergent (LPD-12) LPD-12
3CBA 3CBA Crystal structure of Lipopeptide Detergent (LPD-12) (Hexagonal) LPD-12
6SNC 6SNC crystal structure of LN01 Fab in complex with an HIV-1 gp41 peptide LNO1 Light Chain, LNO1 Heavy Chain, Envelope glycoprotein gp160
6SNC G3DH64 crystal structure of LN01 Fab in complex with an HIV-1 gp41 peptide LNO1 Light Chain, LNO1 Heavy Chain, Envelope glycoprotein gp160
6SND 6SND crystal structure of LN01 Fab in complex with an HIV-1 gp41 peptide LN01 light chain, LN01 heavy chain, Envelope glycoprotein gp160
6SND G3DH64 crystal structure of LN01 Fab in complex with an HIV-1 gp41 peptide LN01 light chain, LN01 heavy chain, Envelope glycoprotein gp160
1K4Y 3219695 Crystal Structure of Rabbit Liver Carboxylesterase in Complex with 4-piperidino-piperidine LIVER CARBOXYLESTERASE (E.C.3.1.1.1)
1LBS P41365 LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) LIPASE B, N-HEXYLPHOSPHONATE ETHYL ESTER
1LBT P41365 LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) LIPASE B, METHYLPENTA(OXYETHYL) HEPTADECANOATE
1THG P22394 1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM LIPASE (E.C.3.1.1.3) TRIACYLGLYCEROL HYDROLASE
1LPA P02703 INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY LIPASE (E.C.3.1.1.3) COMPLEXED WITH COLIPASE AND PHOSPHOLIPID
1LPA P16233 INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY LIPASE (E.C.3.1.1.3) COMPLEXED WITH COLIPASE AND PHOSPHOLIPID
1LPB P02703 THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE PANCREATIC LIPASE COLIPASE COMPLEX INHIBITED BY A C11 ALKYL PHOSPHONATE LIPASE (E.C.3.1.1.3) COMPLEXED WITH COLIPASE AND INHIBITED BY UNDECANE PHOSPHONATE METHYL ESTER (TWO CONFORMATIONS)
1LPB P16233 THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE PANCREATIC LIPASE COLIPASE COMPLEX INHIBITED BY A C11 ALKYL PHOSPHONATE LIPASE (E.C.3.1.1.3) COMPLEXED WITH COLIPASE AND INHIBITED BY UNDECANE PHOSPHONATE METHYL ESTER (TWO CONFORMATIONS)
1LPS P20261 A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF LIPASES LIPASE (E.C.3.1.1.3) COMPLEXED WITH (1S)-MENTHYL HEXYL PHOSPHONATE
1LPO P20261 ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH HEXADECANESULFONATE
1LPP P20261 ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH HEXADECANESULFONATE
1LPN P20261 ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH DODECANESULFONATE
1LPM P20261 A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF LIPASES LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH (1R)-MENTHYL HEXYL PHOSPHONATE
1CRL P20261 INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)
1TCA P41365 THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM CANDIDA ANTARCTICA LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)
1TCB P41365 THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM CANDIDA ANTARCTICA LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)
1TCC P41365 THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM CANDIDA ANTARCTICA LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)
1TRH P20261 TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)
1QPA P11542 LIGNIN PEROXIDASE ISOZYME LIP4.65 (PI 4.65) LIGNIN PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE
1LLP P49012 LIGNIN PEROXIDASE (ISOZYME H2) PI 4.15 LIGNIN PEROXIDASE, HYDROXY GROUP, PROTOPORPHYRIN IX CONTAINING FE

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Supported by JST NBDC Grant Number JPMJND2204

Partly supported by NIH Common Fund Grant #1U01GM125267-01


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Last updated: August 19, 2024