Structure of PDB 1b6a Chain A Binding Site BS02
Receptor Information
>1b6a Chain A (length=355) Species:
9606
(Homo sapiens) [
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KVQTDPPSVPICDLYPNGVFPKGQECEYPEEKKALDQASEEIWNDFREAA
EAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGC
SLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKY
DTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVK
PIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGV
VHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRL
GESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVS
RGDDY
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
1b6a Chain A Residue 482 [
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Receptor-Ligand Complex Structure
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PDB
1b6a
Structure of human methionine aminopeptidase-2 complexed with fumagillin.
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
D251 D262 E459
Binding residue
(residue number reindexed from 1)
D128 D139 E336
Annotation score
3
Enzymatic activity
Catalytic site (original residue number in PDB)
D251 D262 H331 H339 E364 E459
Catalytic site (residue number reindexed from 1)
D128 D139 H208 H216 E241 E336
Enzyme Commision number
3.4.11.18
: methionyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0003723
RNA binding
GO:0004177
aminopeptidase activity
GO:0004239
initiator methionyl aminopeptidase activity
GO:0005515
protein binding
GO:0008235
metalloexopeptidase activity
GO:0046872
metal ion binding
GO:0070006
metalloaminopeptidase activity
Biological Process
GO:0006508
proteolysis
GO:0016485
protein processing
GO:0018206
peptidyl-methionine modification
GO:0031365
N-terminal protein amino acid modification
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0005886
plasma membrane
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1b6a
,
PDBe:1b6a
,
PDBj:1b6a
PDBsum
1b6a
PubMed
9812898
UniProt
P50579
|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)
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