Structure of PDB 5czd Chain A

Receptor sequence
>5czdA (length=301) Species: 1944 (Streptomyces halstedii) [Search protein sequence]
ATAMLFPGMGPAAFSDVGRFMVTNRYTRELLAEADDTLGYSLVDRFRQAE
GDYSEYAQIAFLVNCVALARWAEQTMDLTPRICAGASFGEKSVAAYSGAL
TFADAVRMTAGLARCMDEYFRTEHLGVVTHSFVRAPRERLDEILAELDER
GEWHEISCHIDHDFFMLTLHERNSVWLEGRLRSVGAMPLYAMRPPMHAAA
FGGLRDKAEEEVIAPLTFHDPTLPVVADQDGKVLTTGDEVRTMLLECFVR
PLRWPDVISSLQDQGVTRVCVAGPDSLFGRVGTTTRAFEVIAATPRLALQ
P
3D structure
PDB5czd Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.
ChainA
Resolution2.34 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M28 S106 F107 L131 F220 C266
Catalytic site (residue number reindexed from 1) M9 S87 F88 L112 F201 C247
Enzyme Commision number 2.3.1.39: [acyl-carrier-protein] S-malonyltransferase.
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 PNS A P30 Y72 Y209 M211 S295 P11 Y53 Y190 M192 S276
BS02 1N2 A S106 M135 C266 F267 S87 M116 C247 F248
Gene Ontology
Molecular Function
GO:0004314 [acyl-carrier-protein] S-malonyltransferase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5czd, PDBe:5czd, PDBj:5czd
PDBsum5czd
PubMed26831085
UniProtQ76KY5

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