Structure of PDB 1ocq Chain A

Receptor sequence
>1ocqA (length=300) Species: 76935 (Salipaludibacillus agaradhaerens) [Search protein sequence]
SVVEEHGQLSISNGELVNERGEQVQLKGMSSHGLQWYGQFVNYESMKWLR
DDWGINVFRAAMYTSSGGYIDDPSVKEKVKEAVEAAIDLDIYVIIDWHIL
SDNDPNIYKEEAKDFFDEMSELYGDYPNVIYEIANEPNGSDVTWGNQIKP
YAEEVIPIIRNNDPNNIIIVGTGTWSQDVHHAADNQLADPNVMYAFHFYA
GTHGQNLRDQVDYALDQGAAIFVSEWGTSAATGDGGVFLDEAQVWIDFMD
ERNLSWANWSLTHKDESSAALMPGANPTGGWTEAELSPSGTFVREKIRES
3D structure
PDB1ocq Direct Observation of the Protonation State of an Imino Sugar Glycosidase Inhibitor Upon Binding
ChainA
Resolution1.08 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 IFM A Y66 H101 E139 Y202 E228 A234 T235 G236 W262 Y63 H98 E136 Y199 E225 A231 T232 G233 W259 PDBbind-CN: -logKd/Ki=5.19,Ki=6.5uM
BS02 BGC A H35 Y66 W262 K267 E269 H32 Y63 W259 K264 E266 PDBbind-CN: -logKd/Ki=5.19,Ki=6.5uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ocq, PDBe:1ocq, PDBj:1ocq
PDBsum1ocq
PubMed12812472
UniProtO85465|GUN5_SALAG Endoglucanase 5A (Gene Name=cel5A)

[Back to BioLiP]