Structure of PDB 3qmn Chain X

Receptor sequence
>3qmnX (length=126) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
MIVGLGTDIAEIERVEKALARSGENFARRILTDSELEQFHASKQQGRFLA
KRFAAKEAASKALGTGIAQGVTFHDFTISHDKLGKPLLILSGQAAELASQ
LQVENIHLSISDERHYAMATVILERR
3D structure
PDB3qmn Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
ChainX
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) K61 D112
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 X K51 H80 G84 K85 P86 I110 S111 D112 K51 H80 G84 K85 P86 I110 S111 D112
BS02 COA X R29 E57 K61 G64 T65 G66 I67 R29 E57 K61 G64 T65 G66 I67
BS03 CA X D8 E57 D8 E57
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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