Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7PVO

Adenylosuccinate Synthetase from H. pylori in complex with IMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004019molecular_functionadenylosuccinate synthase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0016874molecular_functionligase activity
A0044208biological_process'de novo' AMP biosynthetic process
A0046040biological_processIMP metabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPcYedKmaR
ChainResidueDetails
AGLY124-ARG135

site_idPS01266
Number of Residues8
DetailsADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG
ChainResidueDetails
AGLN9-GLY16

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AASP12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AHIS40

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AGLY11
AASP12
AGLY39
AARG135
ATHR290
AARG296
ALYS322
ASER400

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AASN37
ATHR121
AGLN215
ATHR230
AARG294

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon