Structure of PDB 7sf2 Chain A

Receptor sequence
>7sf2A (length=586) Species: 537012 (Bacteroides cellulosilyticus DSM 14838) [Search protein sequence]
AQWKPAGDRIKTKWAEQINPSDVLPEYPRPIMQRNDWKNLNGLWDYAIID
KGGRIPTDFEGQILVPFAVESSLSGVGKRVNENQEVIYQRSFEIPSAWRG
KQVLLHFGAVDWKTDVWVNDIKVGSHTGGFTPFSFDITPALSAKGNNRLV
VKVWDPTDRGPQPRGKQVSRPEGIWYTPVTGIWQTVWLEPVAGKHIENLR
ITPDIDRHLLTVKAELNTNSTSDFVEVNVYDGNQLIAAGKSINGEPVEVA
MPENAKLWSPDSPFLYTLKVTLKEGNKIVDKVDSYAAMRKYSTRRDANGI
VRLELNNEALFQFGPLDQGWWPDGLYTAPTDEALLYDIQKTKDFGYNMIR
KHIKVEPARWYTYCDQLGIIVWQDMPSGDRNPQWQNRKYFDGTEMKRSAE
SEAYYRKEWKEIMDCLHSYPCIGTWVPFNEAWGQFKTVEIAEWTKQYDPT
RLVNPASGGNHYTCGDMLDLHNYPAPEMYLYDAQRATVLGEYGGIGLVLK
DHIWEPNRNWGYVQFNSSKEATDEYVKYADMLYKMVDRGFSAAVYTQTTD
VEVEVNGLMTYDRKVIKLDEKRAKEINTRICNSLKK
3D structure
PDB7sf2 Crystal Structure of Beta-Galactosidase from Bacteroides cellulosilyticus
ChainA
Resolution2.75 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 ?
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 MG A D130 D174 Q186 V198 D111 D155 Q167 V179
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7sf2, PDBe:7sf2, PDBj:7sf2
PDBsum7sf2
PubMed
UniProtE2NBY7

[Back to BioLiP]