Structure of PDB 2dq6 Chain A

Receptor sequence
>2dq6A (length=865) Species: 562 (Escherichia coli) [Search protein sequence]
QAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLRLN
GEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAANTA
LEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYPFL
LSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTTRS
GREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMIVAV
DFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHNWTG
NRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQFAE
DASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKGMQ
LYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTVKDDYN
PETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKGGHP
VNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQLTFLM
RHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVLLD
EKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELADE
LLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQFH
EANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQAT
SPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGSGY
LFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLKGLE
NLSGDLYEKITKALA
3D structure
PDB2dq6 Aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli: Crystal structure and conformational change of the methionine 260 residue involved in substrate recognition
ChainA
Resolution1.5 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) E259 H292 E293 H296 E315 N368 Y376
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 H292 H296 E315
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:2dq6, PDBe:2dq6, PDBj:2dq6
PDBsum2dq6
PubMed16885166
UniProtP04825|AMPN_ECOLI Aminopeptidase N (Gene Name=pepN)

[Back to BioLiP]