Structure of PDB 4gys Chain B

Receptor sequence
>4gysB (length=461) Species: 391165 (Granulibacter bethesdensis CGDNIH1) [Search protein sequence]
LSMTLEGIQAFLAQGGTIEQVVTEAYDRITRYGDKAVWIALRPREEVLAE
ARALDASPATGKPLYGVPFAVKDNIDVAGLPCSAACPAFTYEPDRDATVV
ARLRAAGAIVLGKTNLDQFATGLVGTRSPFGAPRCVFDQDYISGGSSSGS
AVAVAAGLVAFSLGTDTAGSGRVPAAFNNLVGVKPTKGLLSTSGVVPACR
SLDCVTVFAASVAEGTLIRRIAEGYDAADPYSRPSQKRRLPHVGLRVGVP
RQDQREFYGNTAYAALYQRALDEMISLDAELVEIDFAPFRDAAKLLYGGP
WVAERLEAVGDHLSRAPDSFDPVVRSIVETAKTLSAVDAFRGQYELAALT
QQANAQWARMDILLLPTAPTIHKVEAVMADPVRLNSQLGHYTNFVNLLDC
AAIAVPAGFIETGLPFGVTLVGPAFSDDSMALIADRLHRRLEPGYGQDRA
SLPDPVLEETN
3D structure
PDB4gys The Structure of Allophanate Hydrolase from Granulibacter bethesdensis Provides Insights into Substrate Specificity in the Amidase Signature Family.
ChainB
Resolution2.201 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K74 S148 S149 T167 T169 A170 G171 S172 V175
Catalytic site (residue number reindexed from 1) K72 S146 S147 T165 T167 A168 G169 S170 V173
Enzyme Commision number 3.5.1.54: allophanate hydrolase.
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 MLI B A122 G124 S148 T169 A170 S172 Y299 R307 A120 G122 S146 T167 A168 S170 Y297 R305
BS02 MLI B S195 G196 V197 R202 S193 G194 V195 R200
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004039 allophanate hydrolase activity
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4gys, PDBe:4gys, PDBj:4gys
PDBsum4gys
PubMed23282241
UniProtQ0BRB0

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