Structure of PDB 7d89 Chain A

Receptor sequence
>7d89A (length=351) Species: 1409 (Bacillus sp. (in: firmicutes)) [Search protein sequence]
QSWRKEANDRILQHRQRELVINVAGIEVEIKQIRHEFAFGSAMNDQVLFN
QTYADFFVQHFNWAVFENEAKWYANEPERGKITYEKADAMLNFANRHQIP
VRGHALFWEVEDANPNWLKSLPNHEVYEAMKRRLEHAGNHFKGKFRHWDV
NNAMMHGSFFKDRFGKQIWKWMYEETKKIDPQALLFVNDYNVISYGEHHA
YKAHINELRQLGAPVEAIGVQGHFADRVDPVVVKERLDVLAELGLPIWVT
AYDSVHPDANRRADNLEALYRVAFSHPAVKGVLMWGFWAGAHWRGEHAAI
VNHDWSLNEAGRRYEKLLQEWTTQRVEVTCPAFHGTYEVRKMLQQQTIEL
D
3D structure
PDB7d89 Insights into the Catalytic Mechanism of a Novel XynA and Structure-Based Engineering for Improving Bifunctional Activities.
ChainA
Resolution2.89384 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
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 CA A E98 K115 E69 K86
BS02 CA A Y219 N220 V221 I222 S223 G251 Y190 N191 V192 I193 S194 G222
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031176 endo-1,4-beta-xylanase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7d89, PDBe:7d89, PDBj:7d89
PDBsum7d89
PubMed34156819
UniProtA0A4P8ESF9

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