Structure of PDB 1boa Chain A Binding Site BS01
Receptor Information
>1boa Chain A (length=354) Species:
9606
(Homo sapiens) [
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KVQTDPPSVPICDLYPNGVFPKGQECEYPEKKALDQASEEIWNDFREAAE
AHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCS
LNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYD
TLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKP
IRNLNGHSIGQYRIHAGKTVPIIKGGEATRMEEGEVYAIETFGSTGKGVV
HDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLG
ESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR
GDDY
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
1boa Chain A Residue 481 [
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Receptor-Ligand Complex Structure
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PDB
1boa
Structure of human methionine aminopeptidase-2 complexed with fumagillin.
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
D262 H331 E364 E459
Binding residue
(residue number reindexed from 1)
D138 H207 E240 E335
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)
D127 D138 H207 H215 E240 E335
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:1boa
,
PDBe:1boa
,
PDBj:1boa
PDBsum
1boa
PubMed
9812898
UniProt
P50579
|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)
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