Structure of PDB 5jfr Chain A

Receptor sequence
>5jfrA (length=366) Species: 9606 (Homo sapiens) [Search protein sequence]
KVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALD
QASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIK
ENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGR
IIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVME
SYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGTRMEEGEVYA
IETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGT
LAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTI
LLRPTCKEVVSRGDDY
3D structure
PDB5jfr Discovery of potent, reversible MetAP2 inhibitors via fragment based drug discovery and structure based drug design-Part 2.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 E252 E347
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 MN A D251 D262 E459 D142 D153 E347
BS02 MN A D262 H331 E364 E459 D153 H222 E252 E347
BS03 6KP A H231 D262 H331 I338 H339 A414 Y444 H122 D153 H222 I229 H230 A302 Y332 MOAD: ic50=5nM
PDBbind-CN: -logKd/Ki=8.30,IC50=5nM
Gene Ontology
Molecular Function
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5jfr, PDBe:5jfr, PDBj:5jfr
PDBsum5jfr
PubMed27136719
UniProtP50579|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)

[Back to BioLiP]