Structure of PDB 1kq0 Chain A

Receptor sequence
>1kq0A (length=354) Species: 9606 (Homo sapiens) [Search protein sequence]
VQTDPPSVPICDLYPNGVFPKGQECEYPEEKKALDQASEEIWNDFREAAE
AHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCS
LNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYD
TLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKP
IRNLNGHSIGQYRIHAGKTVPIIKGGEATRMEEGEVYAIETFGSTGKGVV
HDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLG
ESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR
GDDY
3D structure
PDB1kq0 Human methionine aminopeptidase type 2 in complex with L- and D-methionine
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 ZN A D251 D262 E459 D127 D138 E335
BS02 ZN A D262 H331 E364 E459 D138 H207 E240 E335
BS03 MED A H231 D251 H339 H107 D127 H215
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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Cellular Component
External links
PDB RCSB:1kq0, PDBe:1kq0, PDBj:1kq0
PDBsum1kq0
PubMed16540317
UniProtP50579|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)

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