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2QGA

Plasmodium vivax adenylosuccinate lyase Pv003765 with AMP bound

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
B0006164biological_processpurine nucleotide biosynthetic process
B0006188biological_processIMP biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0009152biological_processpurine ribonucleotide biosynthetic process
B0016829molecular_functionlyase activity
B0044208biological_process'de novo' AMP biosynthetic process
B0046872molecular_functionmetal ion binding
B0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
C0006164biological_processpurine nucleotide biosynthetic process
C0006188biological_processIMP biosynthetic process
C0006189biological_process'de novo' IMP biosynthetic process
C0009152biological_processpurine ribonucleotide biosynthetic process
C0016829molecular_functionlyase activity
C0044208biological_process'de novo' AMP biosynthetic process
C0046872molecular_functionmetal ion binding
C0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA B 901
ChainResidue
BASN279
BASN279
BHOH1236
BHOH1236
BHOH1244
BHOH1244
BHOH1252
BHOH1252

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA C 902
ChainResidue
CASN279
CHOH1256
CHOH1256
CHOH1258
CHOH1258
CHOH1262
CHOH1262
CASN279

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 903
ChainResidue
BARG393
BGLN435
BHOH1071
BHOH1117
BHOH1121
BHOH1291
CLYS219

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 904
ChainResidue
CARG393
CVAL432
CGLN435
CHOH1164
CHOH1253
CHOH1324

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 905
ChainResidue
BTHR167
BHIS168
BSER293
BLYS299
BASN301
BHOH1040
BHOH1053
BHOH1079
CGLN245
CAMP907

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 C 906
ChainResidue
BGLN245
BAMP908
CTHR167
CHIS168
CSER293
CLYS299
CASN301
CHOH1092
CHOH1118
CHOH1255

site_idAC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE AMP C 907
ChainResidue
BARG12
BTYR13
BHIS168
BASN307
BSO4905
BHOH1281
CASN85
CHIS86
CASP87
CSER120
CGLU121
CGLN245
CARG333
CSER338
CTHR339
CARG342
CHOH933
CHOH967
CHOH1007
CHOH1011
CHOH1026
CHOH1115

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR RESIDUE AMP B 908
ChainResidue
BASN85
BHIS86
BASP87
BSER120
BGLU121
BGLN245
BARG333
BSER338
BTHR339
BARG342
BHOH938
BHOH940
BHOH986
BHOH994
BHOH1011
BHOH1086
CARG12
CTYR13
CHIS168
CASN307
CSO4906
CHOH1313

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSstMpHKvN
ChainResidueDetails
BGLY292-ASN301

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PDB entries from 2025-07-16

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