Structure of PDB 5lyx Chain A

Receptor sequence
>5lyxA (length=363) Species: 9606 (Homo sapiens) [Search protein sequence]
KVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSKKALDQA
SEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKEN
GLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRII
DCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESY
EVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVY
AIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFG
TLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHT
ILLRPTCKEVVSR
3D structure
PDB5lyx Novel reversible methionine aminopeptidase-2 (MetAP-2) inhibitors based on purine and related bicyclic templates.
ChainA
Resolution1.9 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) D140 D151 H220 H228 E253 E348
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 7BF A F219 H231 D251 D262 H331 I338 H339 A414 Y444 F108 H120 D140 D151 H220 I227 H228 A303 Y333 MOAD: ic50=0.038uM
PDBbind-CN: -logKd/Ki=7.42,IC50=0.038uM
BS02 MN A D262 H331 E364 E459 D151 H220 E253 E348
BS03 MN A D251 D262 E459 D140 D151 E348
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:5lyx, PDBe:5lyx, PDBj:5lyx
PDBsum5lyx
PubMed27998678
UniProtP50579|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)

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