Structure of PDB 3nfb Chain D

Receptor sequence
>3nfbD (length=364) Species: 364098 (Sphingosinicella xenopeptidilytica) [Search protein sequence]
GPRARDLGVPFEGTPGALNAITDVAGVEVGHTTVISGDGAMVIGKGPYRT
GVTIIHPLGKTSLDGVAAGRAVINGTGEWTGMHLVDEVGQFLGPIALTGT
GNVGLVHQSMMDWSVGKVPEEALFSRLLPVVAETLDNRLNDVFGHGLTRD
HVFAALDGAKGGPVAEGNVGGGTGMIAYTFKGGIGTSSRVVSAGDTRYTV
GVLVQANHGDRNDLRIAGVQIGKEIKGAWPEVIVAAGPDAGKSLLIVIAT
DAPLMPHQLERMARRAALGVGRNGSTAGALSGEFALAFSTSHVIPLGGKP
RLPAIINDTDSETMNALFRGVVQATEEALVNQLVASETMTGANNAKVYGI
PHDQLARIMKARFP
3D structure
PDB3nfb Crystal structure and inhibition of the beta-aminopeptidase BapA, a new ampicillin-recognizing member of the N-terminal nucleophile hydrolase family
ChainD
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L135 N207 S250 S288 G289
Catalytic site (residue number reindexed from 1) L135 N207 S243 S281 G282
Enzyme Commision number 3.4.11.25: beta-peptidyl 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 OAE D F124 L128 F124 L128
BS02 OAE D T76 E133 L135 N207 S250 L287 T76 E133 L135 N207 S243 L280
BS03 OAE D R138 A237 A238 R138 A235 A236
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0042802 identical protein binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0042597 periplasmic space

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Biological Process
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Cellular Component
External links
PDB RCSB:3nfb, PDBe:3nfb, PDBj:3nfb
PDBsum3nfb
PubMed
UniProtQ52VH2|BAPA_SPHXN Beta-peptidyl aminopeptidase BapA (Gene Name=bapA)

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