Structure of PDB 3qmn Chain O

Receptor sequence
>3qmnO (length=127) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
AMIVGLGTDIAEIERVEKALARSGENFARRILTDSELEQFHASKQQGRFL
AKRFAAKEAASKALGTGIAQGVTFHDFTISHDKLGKPLLILSGQAAELAS
QLQVENIHLSISDERHYAMATVILERR
3D structure
PDB3qmn Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
ChainO
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K61 D112
Catalytic site (residue number reindexed from 1) K62 D113
Enzyme Commision number 2.7.8.7: holo-[acyl-carrier-protein] synthase.
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 O K51 H80 L83 G84 K85 P86 I110 S111 D112 K52 H81 L84 G85 K86 P87 I111 S112 D113
BS02 COA O K61 G64 T65 G66 I67 K62 G65 T66 G67 I68
BS03 CA O D8 E57 D9 E58
BS04 A3P O K51 H80 L83 G84 K85 P86 I110 D112 K52 H81 L84 G85 K86 P87 I111 D113
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008897 holo-[acyl-carrier-protein] synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3qmn, PDBe:3qmn, PDBj:3qmn
PDBsum3qmn
PubMed22993090
UniProtQ9KPB6|ACPS_VIBCH Holo-[acyl-carrier-protein] synthase (Gene Name=acpS)

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