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4JA0

Crystal structure of the invertebrate bi-functional purine biosynthesis enzyme PAICS at 2.8 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004638molecular_functionphosphoribosylaminoimidazole carboxylase activity
A0004639molecular_functionphosphoribosylaminoimidazolesuccinocarboxamide synthase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0016874molecular_functionligase activity
A0043727molecular_function5-amino-4-imidazole carboxylate lyase activity
B0004638molecular_functionphosphoribosylaminoimidazole carboxylase activity
B0004639molecular_functionphosphoribosylaminoimidazolesuccinocarboxamide synthase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
B0016874molecular_functionligase activity
B0043727molecular_function5-amino-4-imidazole carboxylate lyase activity
C0004638molecular_functionphosphoribosylaminoimidazole carboxylase activity
C0004639molecular_functionphosphoribosylaminoimidazolesuccinocarboxamide synthase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006164biological_processpurine nucleotide biosynthetic process
C0006189biological_process'de novo' IMP biosynthetic process
C0016831molecular_functioncarboxy-lyase activity
C0016874molecular_functionligase activity
C0043727molecular_function5-amino-4-imidazole carboxylate lyase activity
D0004638molecular_functionphosphoribosylaminoimidazole carboxylase activity
D0004639molecular_functionphosphoribosylaminoimidazolesuccinocarboxamide synthase activity
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006164biological_processpurine nucleotide biosynthetic process
D0006189biological_process'de novo' IMP biosynthetic process
D0016831molecular_functioncarboxy-lyase activity
D0016874molecular_functionligase activity
D0043727molecular_function5-amino-4-imidazole carboxylate lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
APRO31
AGLY32

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
ASER144
AGLU145

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG332
DTYR379

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
ATYR167
AILE205

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
ALYS20
ATHR21
ALYS22
AGLY19

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 506
ChainResidue
AARG104
AGLY109
ASER110
APHE111
AARG217

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
ALYS152
BPRO31
BLYS93

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BARG332
BLYS357
BHOH614

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
BGLY19
BLYS20
BTHR21

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BARG104
BGLY109
BSER110
BARG217
BHOH609

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 501
ChainResidue
CPRO31
CGLY32
CLYS93
DLYS152

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 502
ChainResidue
BTYR379
CARG332
CHOH611

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 C 503
ChainResidue
CLYS20

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 504
ChainResidue
CARG104
CGLY109
CSER110
CARG217

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 501
ChainResidue
DPRO31
DGLY32
DLYS93

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 502
ChainResidue
DARG332
DLYS357

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 503
ChainResidue
DARG104
DTHR108
DGLY109
DSER110
DARG217

Functional Information from PROSITE/UniProt
site_idPS01057
Number of Residues15
DetailsSAICAR_SYNTHETASE_1 SAICAR synthetase signature 1. MIPIEwVTRrlaTGS
ChainResidueDetails
AMET96-SER110

site_idPS01058
Number of Residues9
DetailsSAICAR_SYNTHETASE_2 SAICAR synthetase signature 2. LIDmKIEFG
ChainResidueDetails
ALEU190-GLY198

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PDB entries from 2024-07-17

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