Structure of PDB 1bn5 Chain A

Receptor sequence
>1bn5A (length=355) Species: 9606 (Homo sapiens) [Search protein sequence]
KVQTDPPSVPICDLYPNGVFPKGQECEYPEEKKALDQASEEIWNDFREAA
EAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGC
SLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKY
DTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVK
PIRNLNGHSIGQYRIHAGKTVPIIKGGEATRMEEGEVYAIETFGSTGKGV
VHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRL
GESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVS
RGDDY
3D structure
PDB1bn5 Structure of human methionine aminopeptidase-2 complexed with fumagillin.
ChainA
Resolution1.8 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) D128 D139 H208 H216 E241 E336
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 CO A D251 D262 E459 D128 D139 E336
BS02 CO A D262 H331 E364 E459 D139 H208 E241 E336
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:1bn5, PDBe:1bn5, PDBj:1bn5
PDBsum1bn5
PubMed9812898
UniProtP50579|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)

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