Structure of PDB 4xo5 Chain A

Receptor sequence
>4xo5A (length=866) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
PQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLRL
NGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAANT
ALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYPF
LLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTTR
SGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMIVA
VDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHNWT
GNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQFA
EDASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKGM
QLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTVKDDY
NPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKGGH
PVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQLTFL
MRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVLL
DEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELAD
ELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQF
HEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQA
TSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGSG
YLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLKGL
ENLSGDLYEKITKALA
3D structure
PDB4xo5 Crystal Structure of E. coli Aminopeptidase N in complex with L-Glutamate
ChainA
Resolution1.98 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) E260 H293 E294 H297 E316 N369 Y377
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 H293 H297 E316
BS02 GLU A E121 M260 A262 M263 E264 H297 E298 E320 Y376 Y381 E117 M256 A258 M259 E260 H293 E294 E316 Y372 Y377
BS03 GLU A A638 R641 E642 R686 F690 A634 R637 E638 R682 F686
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:4xo5, PDBe:4xo5, PDBj:4xo5
PDBsum4xo5
PubMed
UniProtP04825|AMPN_ECOLI Aminopeptidase N (Gene Name=pepN)

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