Structure of PDB 2dqm Chain A

Receptor sequence
>2dqmA (length=867) Species: 562 (Escherichia coli) [Search protein sequence]
QPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLR
LNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAAN
TALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYP
FLLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTT
RSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMIV
AVDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHNW
TGNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQF
AEDASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKG
MQLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTVKDD
YNPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKGG
HPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQLTF
LMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVL
LDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELA
DELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQ
FHEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQ
ATSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGS
GYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLKG
LENLSGDLYEKITKALA
3D structure
PDB2dqm Aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli: Crystal structure and conformational change of the methionine 260 residue involved in substrate recognition
ChainA
Resolution1.6 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) 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 BES A E121 M260 G261 A262 E264 V294 H297 E298 H301 E320 Y376 Y381 E118 M257 G258 A259 E261 V291 H294 E295 H298 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2dqm, PDBe:2dqm, PDBj:2dqm
PDBsum2dqm
PubMed16885166
UniProtP04825|AMPN_ECOLI Aminopeptidase N (Gene Name=pepN)

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