Structure of PDB 5vcp Chain A

Receptor sequence
>5vcpA (length=159) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
IREILKMGDPRLLRIADPVDHFDTPELHELVKDMFETMHDANGAGLAAPQ
IGVNLQVVIFGFPPVPETVLINPTITPVSQDMEEGWEGCLSVPGLRGAVS
RFSMIKYHGFDQYGKPIDRVAEGFHARVVQHECDHLIGKLYPMRINDFAK
FGFTEVLFP
3D structure
PDB5vcp Crystal structure of a peptide deformylase from Burkholderia xenovorans in complex with actinonin
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G46 Q51 C99 L100 H141 E142 H145
Catalytic site (residue number reindexed from 1) G45 Q50 C89 L90 H131 E132 H135
Enzyme Commision number 3.5.1.88: peptide deformylase.
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 FE2 A Q51 C99 H141 H145 Q50 C89 H131 H135
BS02 BB2 A G44 A45 G46 Q51 W96 G98 C99 R106 H141 E142 H145 G43 A44 G45 Q50 W86 G88 C89 R96 H131 E132 H135
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0042586 peptide deformylase activity
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0018206 peptidyl-methionine modification

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Molecular Function
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Biological Process
External links
PDB RCSB:5vcp, PDBe:5vcp, PDBj:5vcp
PDBsum5vcp
PubMed
UniProtQ13XB1

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