Structure of PDB 4xmw Chain A

Receptor sequence
>4xmwA (length=867) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLR
LNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAAN
TALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYP
FLLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTT
RSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMIV
AVDFFNAGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHNW
TGNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQF
AEDASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKG
MQLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTVKDD
YNPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKGG
HPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQLTF
LMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVL
LDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELA
DELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQ
FHEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQ
ATSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGS
GYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLKG
LENLSGDLYEKITKALA
3D structure
PDB4xmw Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-aspartic acid
ChainA
Resolution2.2 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) E264 H297 E298 H301 E320 N373 Y381
Catalytic site (residue number reindexed from 1) E261 H294 E295 H298 E317 N370 Y378
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 H294 H298 E317
BS02 ASP A A260 A262 H297 E298 E320 Y376 Y381 A257 A259 H294 E295 E317 Y373 Y378
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4xmw, PDBe:4xmw, PDBj:4xmw
PDBsum4xmw
PubMed
UniProtP04825|AMPN_ECOLI Aminopeptidase N (Gene Name=pepN)

[Back to BioLiP]