Structure of PDB 1r5h Chain A

Receptor sequence
>1r5hA (length=369) Species: 9606 (Homo sapiens) [Search protein sequence]
KVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALD
QASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIK
ENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGR
IIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVME
SYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIIKGGEATRMEEGE
VYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINEN
FGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFE
HTILLRPTCKEVVSRGDDY
3D structure
PDB1r5h 3-Amino-2-hydroxyamides and related compounds as inhibitors of methionine aminopeptidase-2.
ChainA
Resolution2.4 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 E255 E350
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 E350
BS02 MN A D262 H331 E364 E459 D153 H222 E255 E350
BS03 AO2 A F219 H231 D251 D262 L328 N329 H331 H339 E364 M384 Y444 E459 F110 H122 D142 D153 L219 N220 H222 H230 E255 M275 Y335 E350 MOAD: ic50=0.17uM
PDBbind-CN: -logKd/Ki=6.74,IC50=0.18uM
BindingDB: IC50=170nM
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:1r5h, PDBe:1r5h, PDBj:1r5h
PDBsum1r5h
PubMed15012983
UniProtP50579|MAP2_HUMAN Methionine aminopeptidase 2 (Gene Name=METAP2)

[Back to BioLiP]