Structure of PDB 2vav Chain K

Receptor sequence
>2vavK (length=341) Species: 5044 (Hapsidospora chrysogena) [Search protein sequence]
NRFEASLDAQDIARISLFTLESGVILRDVPVAYKSWGRMNVSRDNCVIVC
HTLTSSAHVTSWWPTLFGQGRAFDTSRYFIICLNYLGSPFGSAGPCSPDP
YGAKFPRTTIRDDVRIHRQVLDRLGVRQIAAVVGASMGGMHTLEWAFFGP
EYVRKIVPIATSCRQSGWCAAWFETQRQCIYDDPKYLDGEYDVDDQPVRG
LETARKIANLTYKSKPAMDERFHMGQPIEAVSSYLRYQAQKFAASFDANC
YIAMTLKFDTHDISRGRAGSIPEALAMITQPALIICARSDGLYSFDEHVE
MGRSIPNSRLCVVDTNEGHDFFVMEADKVNDAVRGFLDQSL
3D structure
PDB2vav The last step in cephalosporin C formation revealed: crystal structures of deacetylcephalosporin C acetyltransferase from Acremonium chrysogenum in complexes with reaction intermediates.
ChainK
Resolution2.5 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 CSC K T58 T60 S149 R218 Y225 K226 R234 Q281 F365 V366 T52 T54 S136 R205 Y212 K213 R221 Q238 F322 V323
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:2vav, PDBe:2vav, PDBj:2vav
PDBsum2vav
PubMed18279889
UniProtP39058|CEFG_HAPCH Acetyl-CoA--deacetylcephalosporin C acetyltransferase (Gene Name=CEFG)

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