Structure of PDB 1c23 Chain A Binding Site BS02
Receptor Information
>1c23 Chain A (length=262) Species:
562
(Escherichia coli) [
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AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGQGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHD
Ligand information
Ligand ID
CO
InChI
InChI=1S/Co/q+2
InChIKey
XLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341
[Co++]
Formula
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
1c23 Chain A Residue 402 [
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Receptor-Ligand Complex Structure
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PDB
1c23
Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
D97 D108 E235
Binding residue
(residue number reindexed from 1)
D96 D107 E234
Annotation score
3
Enzymatic activity
Catalytic site (original residue number in PDB)
H79 D97 D108 H171 Q175 H178 Q182 E204 N208 Q233 E235
Catalytic site (residue number reindexed from 1)
H78 D96 D107 H170 Q174 H177 Q181 E203 N207 Q232 E234
Enzyme Commision number
3.4.11.18
: methionyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0004177
aminopeptidase activity
GO:0004239
initiator methionyl aminopeptidase activity
GO:0008198
ferrous iron binding
GO:0008235
metalloexopeptidase activity
GO:0046872
metal ion binding
GO:0046914
transition metal ion binding
GO:0070006
metalloaminopeptidase activity
Biological Process
GO:0006508
proteolysis
Cellular Component
GO:0005829
cytosol
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1c23
,
PDBe:1c23
,
PDBj:1c23
PDBsum
1c23
PubMed
10555963
UniProt
P0AE18
|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)
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