Structure of PDB 4xo4 Chain A

Receptor sequence
>4xo4A (length=870) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MTQQPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDA
PLRLNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISP
AANTALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKI
KYPFLLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDT
FTTRSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIY
MIVAVDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYF
HNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRG
LQFAEDASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENF
QKGMQLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTV
KDDYNPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQ
KGGHPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQ
LTFLMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFR
AVLLDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLAT
ELADELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLV
SKQFHEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWF
ILQATSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAE
DGSGYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQ
LKGLENLSGDLYEKITKALA
3D structure
PDB4xo4 Crystal Structure of E. coli Aminopeptidase N in complex with L-Methionine
ChainA
Resolution2.18 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) E264 H297 E298 H301 E320 N373 Y381
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 H297 H301 E320
BS02 MET A R728 D729 Q753 R728 D729 Q753
BS03 MET A D452 Y454 Q527 P528 D452 Y454 Q527 P528
BS04 MET A E121 M260 A262 E264 H297 E298 E320 Y376 Y381 E121 M260 A262 E264 H297 E298 E320 Y376 Y381
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:4xo4, PDBe:4xo4, PDBj:4xo4
PDBsum4xo4
PubMed
UniProtP04825|AMPN_ECOLI Aminopeptidase N (Gene Name=pepN)

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