Structure of PDB 4flj Chain A

Receptor sequence
>4fljA (length=304) Species: 9606 (Homo sapiens) [Search protein sequence]
YRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKL
LSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCY
PSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHG
DLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHA
QANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKSGHVFTIEPMI
CEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTDTGCEILTRRLDSARP
HFMS
3D structure
PDB4flj Structural analysis of bengamide derivatives as inhibitors of methionine aminopeptidases.
ChainA
Resolution1.74 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D229 D240 H303 H310 E336 E367
Catalytic site (residue number reindexed from 1) D140 D151 H214 H221 E247 E278
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 D240 H303 T334 E336 E367 D151 H214 T245 E247 E278
BS02 MN A D229 D240 E367 D140 D151 E278
BS03 Y08 A Y195 H212 D229 D240 C301 H303 F309 H310 E336 E367 Y106 H123 D140 D151 C212 H214 F220 H221 E247 E278 MOAD: ic50=7.45uM
PDBbind-CN: -logKd/Ki=5.13,IC50=7.45uM
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:4flj, PDBe:4flj, PDBj:4flj
PDBsum4flj
PubMed22913487
UniProtP53582|MAP11_HUMAN Methionine aminopeptidase 1 (Gene Name=METAP1)

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