Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

BioLiP

Structure of PDB 4qhp Chain A

Receptor sequence
>4qhpA (length=866) Species: 487 (Neisseria meningitidis) [Search protein sequence]
SKTVHYLKDYQTPAYHILKTDLHFDINEPQTVVKSRLTVEPQRVGEPLVL
DGSAKLLSVKINGAAADYVLEGETLTIAGVPSERFTVEVETEILPAENKS
LMGLYASGGNLFTQCEPEGFRKITFYIDRPDVMSKFTTTIVADKKRYPVL
LSNGNKIDGGEFSDGRHWVKWEDPFSKPSYLFALVAGDLAVTEDYFTTMS
GRNVKIEFYTTEADKPKVGFAVESLKNAMKWDETRFGLEYDLDIFMVVAV
GDFNMGAMENKGLNIFNTKFVLADSRTATDTDFEGIESVVGHEYFHNWTG
NRVTCRDWFQLSLKEGLTVFRDQEFSGDRASRAVRRIENIRLLRQHQFPE
DAGPTAHPVRPASYEEMNNFYTMTVYEKGAEVVRMYHTLLGEEGFQKGMK
LYFQRHDGQAVTCDDFRAAMADANGINLDQFALWYSQAGTPVLEAEGRLK
NNIFELTVKQTVPPTPDMTDKQPMMIPVKVGLLNRNGEAVAFDYQGKRAT
EAVLLLTEAEQTFLLEGVTEAVVPSLLRGFSAPVHLNYPYSDDDLLLLLA
HDSDAFTRWEAAQTLYRRAVAANLATLSDGVELPKHEKLLAAVEKVISDD
LLDNAFKALLLGVPSEAELWDGAENIDPLRYHQAREALLDTLAVHFLPKW
HELNRQAAKQENQSYEYSPEAAGWRTLRNVCRAFVLRADPAHIETVAEKY
GEMAQNMTHEWGILSAVNGNESDTRNRLLAQFADKFSDDALVMDKYFALV
GSSRRSDTLQQVRTALQHPKFSLENPNKARSLIGSFSRNVPHFHAEDGSG
YRFIADKVIEIDRFNPQVAARLVQAFNLCNKLEPHRKNLVKQALQRIRAQ
EGLSKDVGEIVGKILD
3D structure
PDB4qhp Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.
ChainA
Resolution1.6 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) E260 H293 E294 H297 E316 N369 Y377
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 32Q A Q115 E117 M256 G257 A258 M259 E260 H293 E294 H297 E316 D323 Y377 Q114 E116 M255 G256 A257 M258 E259 H292 E293 H296 E315 D322 Y376 MOAD: Ki=9nM
PDBbind-CN: -logKd/Ki=8.05,Ki=9.0nM
BS02 32R A N156 P175 F176 R203 D242 L243 D244 N155 P174 F175 R202 D241 L242 D243 MOAD: Ki=9nM
BS03 ZN A H293 H297 E316 H292 H296 E315
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
View graph for
Biological Process
External links

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417