Structure of PDB 2vh9 Chain B

Receptor sequence
>2vh9B (length=266) Species: 4020 (Tropaeolum majus) [Search protein sequence]
QGPPSPGYYPSSQITSLGFDQGYTNLWGPQHQRVDQGSLTIWLDSTSGSG
FKSINRYRSGYFGANIKLQSGYTAGVITSFYLSNNQDYPGKHDEIDIEFL
GTIPGKPYTLQTNVFIEGSGDREMRIHLWFDPTQDYHNYAIYWTPSEIIF
FVDDVPIRRYPRKSDATFPLRPLWVYGSVWDASSWATENGKYKADYRYQP
FVGKYEDFKLGSCTVEAASSCNPASVSPYGQLSQQQVAAMEWVQKNYMVY
NYCDDPTRDHTLTPEC
3D structure
PDB2vh9 Analysis of Nasturtium Tmnxg1 Complexes by Crystallography and Molecular Dynamics Provides Detailed Insight Into Substrate Recognition by Family Gh16 Xyloglucan Endo-Transglycosylases and Endo-Hydrolases.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E94 D96 E98
Catalytic site (residue number reindexed from 1) E94 D96 E98
Enzyme Commision number 2.4.1.207: xyloglucan:xyloglucosyl transferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 XYS B Y88 P89 Y88 P89
BS02 BGC B W27 Y81 S178 W180 W27 Y81 S178 W180
BS03 XYS B L26 N85 L26 N85
BS04 ZN B D259 T261 D259 T261
BS05 BGC B Y81 E94 E98 W180 Y81 E94 E98 W180
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016762 xyloglucan:xyloglucosyl transferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0010411 xyloglucan metabolic process
GO:0042546 cell wall biogenesis
GO:0044042 glucan metabolic process
Cellular Component
GO:0005618 cell wall
GO:0048046 apoplast

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2vh9, PDBe:2vh9, PDBj:2vh9
PDBsum2vh9
PubMed19004021
UniProtQ07524

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