Structure of PDB 6wqv Chain B

Receptor sequence
>6wqvB (length=346) Species: 1161942 (Ruminococcus champanellensis) [Search protein sequence]
TQMRDLTASQLLDEITIGWNLGNTLDATTTSWLPNPTPAQSETAWGCPMT
TKAMIDKVKEGGFNTVRVPVSWIDHTGSAPEYQIDEAWMNRVQEVVNYVI
DNDMYCILNIHHENDWLIPTNAQKDSVNARLDAIWTQIATRFGSYDEHLI
FEGMNQPRLVGDPNEWNGGNQEARQVINSYNQTFVNTVRATGGNNAIRCL
MVPTYAASCSSTTVNDFVLPTDTVANKLIVDIHSYSPYNFALNTSGTSSF
TQSDISQLQWTLQEIYNSFGAKGIPVIIGQFGALNKNNINGRVLWGENYL
RIAKSYNIRCIWWDNNAFDTSGENFGLLNRGTLTWQYPELLEAMMK
3D structure
PDB6wqv A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis.
ChainB
Resolution1.45 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.2.1.4: cellulase.
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 GLC B H119 H120 N163 Q164 H241 Y243 Q288 W321 E331 H111 H112 N155 Q156 H233 Y235 Q280 W313 E323
BS02 BGC B N31 H120 W321 N323 E331 N23 H112 W313 N315 E323
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0000272 polysaccharide catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6wqv, PDBe:6wqv, PDBj:6wqv
PDBsum6wqv
PubMed33454012
UniProtD4LAX7

[Back to BioLiP]