Structure of PDB 5lyw Chain A

Receptor sequence
>5lywA (length=359) Species: 9606 (Homo sapiens) [Search protein sequence]
KVQTDPPSVPICDLYPNGVFPKGQECEYPTAAWRTTSEEKKALDQASEEI
WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNA
GLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAF
TVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEI
DGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGATRMEEGEVYAIETFG
STGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCR
RWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPT
CKEVVSRGD
3D structure
PDB5lyw Novel reversible methionine aminopeptidase-2 (MetAP-2) inhibitors based on purine and related bicyclic templates.
ChainA
Resolution1.69 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) D136 D147 H216 H224 E247 E342
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 7BH A F219 H231 D251 D262 H331 I338 H339 M384 Y444 F104 H116 D136 D147 H216 I223 H224 M267 Y327 MOAD: ic50=0.7uM
PDBbind-CN: -logKd/Ki=6.15,IC50=0.7uM
BS02 MN A D262 H331 E364 E459 D147 H216 E247 E342
BS03 MN A D251 D262 E459 D136 D147 E342
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:5lyw, PDBe:5lyw, PDBj:5lyw
PDBsum5lyw
PubMed27998678
UniProtP50579|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)

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