Structure of PDB 3b3w Chain A

Receptor sequence
>3b3wA (length=291) Species: 671 (Vibrio proteolyticus) [Search protein sequence]
MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIA
SEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDS
TIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAA
EEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACADHASWHNAGYPAAMPFESKFND
YNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
3D structure
PDB3b3w Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus.
ChainA
Resolution1.75 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) H97 D117 E151 E152 D179 H256
Catalytic site (residue number reindexed from 1) H97 D117 E151 E152 D179 H256
Enzyme Commision number 3.4.11.10: bacterial leucyl aminopeptidase.
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 ZN A D117 E152 H256 D117 E152 H256
BS02 ZN A H97 D117 D179 H97 D117 D179
BS03 LEU A D117 E151 E152 D179 C227 H256 D117 E151 E152 D179 C227 H256 PDBbind-CN: -logKd/Ki=4.19,Ki=65uM
Gene Ontology
Molecular Function
GO:0008235 metalloexopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3b3w, PDBe:3b3w, PDBj:3b3w
PDBsum3b3w
PubMed18576673
UniProtQ01693|AMPX_VIBPR Bacterial leucyl aminopeptidase

[Back to BioLiP]