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

1DJ2

STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM AESTIVUM AND ARABIDOPSIS THALIANA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004019molecular_functionadenylosuccinate synthase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006167biological_processAMP biosynthetic process
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0009570cellular_componentchloroplast stroma
A0016874molecular_functionligase activity
A0044208biological_process'de novo' AMP biosynthetic process
A0046872molecular_functionmetal ion binding
A0048046cellular_componentapoplast
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004019molecular_functionadenylosuccinate synthase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006167biological_processAMP biosynthetic process
B0009507cellular_componentchloroplast
B0009536cellular_componentplastid
B0009570cellular_componentchloroplast stroma
B0016874molecular_functionligase activity
B0044208biological_process'de novo' AMP biosynthetic process
B0046872molecular_functionmetal ion binding
B0048046cellular_componentapoplast
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GDP A 500
ChainResidue
AGLY30
ATYR62
ALYS349
AASP351
AGLY432
AILE433
AGLY434
AASP31
AGLY33
ALYS34
AGLY35
ALYS36
AGLY58
AHIS59
ATHR60

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GDP B 600
ChainResidue
BGLY30
BASP31
BGLY33
BLYS34
BGLY35
BLYS36
BGLY58
BHIS59
BTHR60
BTYR62
BLYS349
BASP351
BGLY432
BILE433
BGLY434
BPRO435

Functional Information from PROSITE/UniProt
site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYssKviR
ChainResidueDetails
AGLY151-ARG162

site_idPS01266
Number of Residues8
DetailsADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG
ChainResidueDetails
AGLN28-GLY35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03125
ChainResidueDetails
AASP31
BASP31

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_03125
ChainResidueDetails
AHIS59
BHIS59

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY30
ALYS349
AGLY432
BGLY30
BLYS349
BGLY432

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03125
ChainResidueDetails
AASP31
BARG323
AGLY58
AARG162
ATHR317
AARG323
BASP31
BGLY58
BARG162
BTHR317

site_idSWS_FT_FI5
Number of Residues10
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03125
ChainResidueDetails
AASN56
BARG321
ATHR148
AGLN242
ATHR257
AARG321
BASN56
BTHR148
BGLN242
BTHR257

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gim
ChainResidueDetails
AGLN242
AASP31
AHIS59

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gim
ChainResidueDetails
BGLN242
BASP31
BHIS59

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon