Structure of PDB 5mft Chain A

Receptor sequence
>5mftA (length=868) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QQPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPL
RLNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAA
NTALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKY
PFLLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFT
TRSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMI
VAVDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHN
WTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQ
FAEDASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQK
GMQLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTVKD
DYNPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKG
GHPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQLT
FLMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAV
LLDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATEL
ADELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSK
QFHEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFIL
QATSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDG
SGYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLK
GLENLSGDLYEKITKALA
3D structure
PDB5mft Insight into the remarkable affinity and selectivity of the aminobenzosuberone scaffold for the M1 aminopeptidases family based on structure analysis.
ChainA
Resolution1.59 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E264 H297 E298 H301 E320 N373 Y381
Catalytic site (residue number reindexed from 1) E262 H295 E296 H299 E318 N371 Y379
Enzyme Commision number 3.4.11.2: membrane alanyl 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 ZN A H297 H301 E320 H295 H299 E318
BS02 7MF A E121 M260 E264 H297 E298 H301 E320 Y376 Y381 E119 M258 E262 H295 E296 H299 E318 Y374 Y379 MOAD: Ki=34nM
PDBbind-CN: -logKd/Ki=7.47,Ki=34nM
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0005515 protein binding
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5mft, PDBe:5mft, PDBj:5mft
PDBsum5mft
PubMed28383176
UniProtP04825|AMPN_ECOLI Aminopeptidase N (Gene Name=pepN)

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