Structure of PDB 5yq1 Chain A

Receptor sequence
>5yq1A (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
PDB5yq1 Crystal structure of E.coli aminopeptidase N in complex with O-Methyl-L-tyrosine
ChainA
Resolution1.58 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) 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 0A1 A Q119 E121 M260 A262 M263 E264 H297 E298 E320 Y376 Y381 Q115 E117 M256 A258 M259 E260 H293 E294 E316 Y372 Y377
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:5yq1, PDBe:5yq1, PDBj:5yq1
PDBsum5yq1
PubMed
UniProtP04825|AMPN_ECOLI Aminopeptidase N (Gene Name=pepN)

[Back to BioLiP]