Structure of PDB 7a15 Chain A

Receptor sequence
>7a15A (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
KVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALD
QASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIK
ENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGR
IIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVME
SYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVATRMEEGEVYAI
ETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTL
AFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTIL
LRPTCKEVVSRGDDY
3D structure
PDB7a15 Structure-based optimisation of orally active & reversible MetAP-2 inhibitors maintaining a tight 'molecular budget'.
ChainA
Resolution2.15 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) D142 D153 H222 H230 E251 E346
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 QV5 A F219 H231 H331 I338 H339 H382 Y383 M384 A414 Y444 F110 H122 H222 I229 H230 H269 Y270 M271 A301 Y331 MOAD: ic50=0.00000001M
BS02 MN A D251 D262 E459 D142 D153 E346
BS03 MN A D262 H331 E364 E459 D153 H222 E251 E346
Gene Ontology
Molecular Function
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:7a15, PDBe:7a15, PDBj:7a15
PDBsum7a15
PubMed32919012
UniProtP50579|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)

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