Structure of PDB 4qir Chain A

Receptor sequence
>4qirA (length=864) Species: 122586 (Neisseria meningitidis MC58) [Search protein sequence]
TVHYLKDYQTPAYHILKTDLHFDINEPQTVVKSRLTVEPQRVGEPLVLDG
SAKLLSVKINGAAADYVLEGETLTIAGVPSERFTVEVETEILPAENKSLM
GLYASGGNLFTQCEPEGFRKITFYIDRPDVMSKFTTTIVADKKRYPVLLS
NGNKIDGGEFSDGRHWVKWEDPFSKPSYLFALVAGDLAVTEDYFTTMSGR
NVKIEFYTTEADKPKVGFAVESLKNAMKWDETRFGLEYDLDIFMVVAVGD
FNMGAMENKGLNIFNTKFVLADSRTATDTDFEGIESVVGHEYFHNWTGNR
VTCRDWFQLSLKEGLTVFRDQEFSGDRASRAVRRIENIRLLRQHQFPEDA
GPTAHPVRPASYEEMNNFYTMTVYEKGAEVVRMYHTLLGEEGFQKGMKLY
FQRHDGQAVTCDDFRAAMADANGINLDQFALWYSQAGTPVLEAEGRLKNN
IFELTVKQTVPPTPDMTDKQPMMIPVKVGLLNRNGEAVAFDYQGKRATEA
VLLLTEAEQTFLLEGVTEAVVPSLLRGFSAPVHLNYPYSDDDLLLLLAHD
SDAFTRWEAAQTLYRRAVAANLATLSDGVELPKHEKLLAAVEKVISDDLL
DNAFKALLLGVPSEAELWDGAENIDPLRYHQAREALLDTLAVHFLPKWHE
LNRQAAKQENQSYEYSPEAAGWRTLRNVCRAFVLRADPAHIETVAEKYGE
MAQNMTHEWGILSAVNGNESDTRNRLLAQFADKFSDDALVMDKYFALVGS
SRRSDTLQQVRTALQHPKFSLENPNKARSLIGSFSRNVPHFHAEDGSGYR
FIADKVIEIDRFNPQVAARLVQAFNLCNKLEPHRKNLVKQALQRIRAQEG
LSKDVGEIVGKILD
3D structure
PDB4qir Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.
ChainA
Resolution1.701 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E260 H293 E294 H297 E316 N369 Y377
Catalytic site (residue number reindexed from 1) E257 H290 E291 H294 E313 N366 Y374
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 379 A E117 M256 G257 A258 M259 E260 H293 E294 H297 E316 D323 N369 Y372 Y377 E114 M253 G254 A255 M256 E257 H290 E291 H294 E313 D320 N366 Y369 Y374 MOAD: Ki=112nM
PDBbind-CN: -logKd/Ki=6.95,Ki=112nM
BS02 ZN A H293 H297 E316 H290 H294 E313
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:4qir, PDBe:4qir, PDBj:4qir
PDBsum4qir
PubMed25192493
UniProtQ9JYV4

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