Structure of PDB 1qd6 Chain C

Receptor sequence
>1qd6C (length=240) Species: 562 (Escherichia coli) [Search protein sequence]
FTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWR
GILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFA
GWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVV
GNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSY
PITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF
3D structure
PDB1qd6 Structural evidence for dimerization-regulated activation of an integral membrane phospholipase.
ChainC
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S106 H142 S144 G146 R147 S152 N156
Catalytic site (residue number reindexed from 1) S77 H113 S115 G117 R118 S123 N127
Enzyme Commision number 3.1.1.32: phospholipase A1.
3.1.1.4: phospholipase A2.
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 peptide C Y33 Y35 R79 N85 F119 D135 M163 H202 F269 Y4 Y6 R50 N56 F90 D106 M134 H173 F240
BS02 peptide C K233 H234 K204 H205
BS03 CA C R147 S152 R118 S123
BS04 HDS C Y92 Y114 H142 S144 G146 Y63 Y85 H113 S115 G117
BS05 HDS C L40 L71 W98 F109 L265 L11 L42 W69 F80 L236
Gene Ontology
Molecular Function
GO:0004620 phospholipase activity
Biological Process
GO:0006629 lipid metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qd6, PDBe:1qd6, PDBj:1qd6
PDBsum1qd6
PubMed10537112
UniProtP0A921|PA1_ECOLI Phospholipase A1 (Gene Name=pldA)

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