Structure of PDB 4ak7 Chain A

Receptor sequence
>4ak7A (length=369) Species: 310297 (Phocaeicola plebeius) [Search protein sequence]
NYDERKADSLGIPKGNKLSAAMKRAMKWENHDNKWFFEYKMEPLKGDLAY
EEGVVRRDPSAMLKIGDTYYVWYSKSYGPTQGFAGDIEKDKVFPWDRCDI
WYATSKDGLTWKEQGIAVKRGEKGAYDDRSVFTPEVMEWKGKYYLCYQAV
KSPYTVRVKNTIGMACADSPEGLWTKTDKPVLEPSDTGEWEGDEDNRFKV
VSKGDFDSHKVHDPCIIPYNGKFYMYYKGERMGEEITWGGREIKHGVAIA
ENPMGPYVKSEYNPISNSGHQVCVWPYKGGIASLITTDGPEKNTLQWSPD
GINFEIMSVVKGAPHAIGLNRSADAEKEPTEILRWGLTHIYNSSDYQSIM
RFSTWTLQTHTAKGESKER
3D structure
PDB4ak7 Analysis of Keystone Enzyme in Agar Hydrolysis Provides Insight Into the Degradation (of a Polysaccharide from) Red Seaweeds.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) I44
Catalytic site (residue number reindexed from 1) I12
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 47N A W127 T165 Q180 H244 D245 K260 E262 R273 H302 Q303 W95 T133 Q148 H212 D213 K228 E230 R241 H270 Q271
BS02 CA A Y186 N192 K242 H244 Y154 N160 K210 H212
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ak7, PDBe:4ak7, PDBj:4ak7
PDBsum4ak7
PubMed22393053
UniProtB5CY74

[Back to BioLiP]