Structure of PDB 2vfc Chain B

Receptor sequence
>2vfcB (length=271) Species: 1781 (Mycobacterium marinum) [Search protein sequence]
DLTGYLDRINYGATDPTLDVLRDLVSAHTGAIAFENLDPLMGVPVDDLSA
EALADKLVDRRRGGYCYEHNGLIGYVLAELGYRVRRLAGRVVWLAPPDAP
TPAQTHTVLAVTFPGCQGPYLVDVGFGGMTPTAPLRLETGTVQQTALEPY
RLDDRGDGLVLQAMVRDEWQALYEFSTLTRPQVDLRVGSWFVSTHPTSHF
VTGLMAATVADDARWNLMGRNLAIHRRGGTEKILLEDAAAVVDTLGDRFG
INVADVGERGRLEARIDKVCF
3D structure
PDB2vfc Divergence of Cofactor Recognition Across Evolution: Coenzyme a Binding in a Prokaryotic Arylamine N-Acetyltransferase.
ChainB
Resolution2.7 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) E39 R65 C70 H110 D127
Catalytic site (residue number reindexed from 1) E35 R61 C66 H106 D123
Enzyme Commision number 2.3.1.5: arylamine N-acetyltransferase.
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 COA B F38 Y69 C70 F130 G131 E152 V169 F204 N220 M222 H229 K236 F34 Y65 C66 F126 G127 E148 V165 F200 N216 M218 H225 K232
Gene Ontology
Molecular Function
GO:0016407 acetyltransferase activity
GO:0016740 transferase activity

View graph for
Molecular Function
External links
PDB RCSB:2vfc, PDBe:2vfc, PDBj:2vfc
PDBsum2vfc
PubMed18005984
UniProtB2HIZ6

[Back to BioLiP]