Structure of PDB 2vat Chain G

Receptor sequence
>2vatG (length=342) Species: 5044 (Hapsidospora chrysogena) [Search protein sequence]
NRFEASLDAQDIARISLFTLESGVILRDVPVAYKSWGRMNVSRDNCVIVC
HTLTSSAHVTSWWPTLFGQGRAFDTSRYFIICLNYLGSPFGSAGPCSPDP
DARPYGAKFPRTTIRDDVRIHRQVLDRLGVRQIAAVVGASMGGMHTLEWA
FFGPEYVRKIVPIATSCRQSGWCAAWFETQRQCIYDDPKYLDGEYDVDDQ
PVRGLETARKIANLTYKSKPAMDERFHMQPIEAVSSYLRYQAQKFAASFD
ANCYIAMTLKFDTHDISRGRAGSIPEALAMITQPALIICARSDGLYSFDE
HVEMGRSIPNSRLCVVDTNEGHDFFVMEADKVNDAVRGFLDQ
3D structure
PDB2vat The Last Step in Cephalosporin C Formation Revealed: Crystal Structures of Deacetylcephalosporin C Acetyltransferase from Acremonium Chrysogenum in Complexes with Reaction Intermediates.
ChainG
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.175: deacetylcephalosporin-C 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 G Y225 S276 Y277 Y280 Q281 D363 F365 V366 M367 Y216 S236 Y237 Y240 Q241 D323 F325 V326 M327
Gene Ontology
Molecular Function
GO:0004414 homoserine O-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0033813 deacetylcephalosporin-C acetyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0009092 homoserine metabolic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2vat, PDBe:2vat, PDBj:2vat
PDBsum2vat
PubMed18279889
UniProtP39058|CEFG_HAPCH Acetyl-CoA--deacetylcephalosporin C acetyltransferase (Gene Name=CEFG)

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