Structure of PDB 2evm Chain A Binding Site BS02
Receptor Information
>2evm Chain A (length=259) Species:
562
(Escherichia coli) [
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SIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQ
HAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKD
GFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAI
QKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTI
EPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKD
DTIPAIISH
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
2evm Chain A Residue 902 [
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Receptor-Ligand Complex Structure
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PDB
2evm
Structural analysis of metalloform-selective inhibition of methionine aminopeptidase.
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
D108 H171 T202 E204 E235
Binding residue
(residue number reindexed from 1)
D105 H168 T199 E201 E232
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
H79 D97 D108 H171 R175 H178 Q182 E204 N208 Q233 E235
Catalytic site (residue number reindexed from 1)
H76 D94 D105 H168 R172 H175 Q179 E201 N205 Q230 E232
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:2evm
,
PDBe:2evm
,
PDBj:2evm
PDBsum
2evm
PubMed
16552144
UniProt
P0AE18
|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)
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