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2VD6

Human adenylosuccinate lyase in complex with its substrate N6-(1,2- Dicarboxyethyl)-AMP, and its products AMP and fumarate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0003824molecular_functioncatalytic activity
A0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006167biological_processAMP biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0007584biological_processresponse to nutrient
A0009060biological_processaerobic respiration
A0009152biological_processpurine ribonucleotide biosynthetic process
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0014850biological_processresponse to muscle activity
A0016829molecular_functionlyase activity
A0032991cellular_componentprotein-containing complex
A0042594biological_processresponse to starvation
A0042802molecular_functionidentical protein binding
A0044208biological_process'de novo' AMP biosynthetic process
A0044209biological_processAMP salvage
A0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
A0097294biological_process'de novo' XMP biosynthetic process
B0001666biological_processresponse to hypoxia
B0003824molecular_functioncatalytic activity
B0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006167biological_processAMP biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0007584biological_processresponse to nutrient
B0009060biological_processaerobic respiration
B0009152biological_processpurine ribonucleotide biosynthetic process
B0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
B0014850biological_processresponse to muscle activity
B0016829molecular_functionlyase activity
B0032991cellular_componentprotein-containing complex
B0042594biological_processresponse to starvation
B0042802molecular_functionidentical protein binding
B0044208biological_process'de novo' AMP biosynthetic process
B0044209biological_processAMP salvage
B0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
B0097294biological_process'de novo' XMP biosynthetic process
C0001666biological_processresponse to hypoxia
C0003824molecular_functioncatalytic activity
C0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
C0005829cellular_componentcytosol
C0006164biological_processpurine nucleotide biosynthetic process
C0006167biological_processAMP biosynthetic process
C0006177biological_processGMP biosynthetic process
C0006189biological_process'de novo' IMP biosynthetic process
C0007584biological_processresponse to nutrient
C0009060biological_processaerobic respiration
C0009152biological_processpurine ribonucleotide biosynthetic process
C0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
C0014850biological_processresponse to muscle activity
C0016829molecular_functionlyase activity
C0032991cellular_componentprotein-containing complex
C0042594biological_processresponse to starvation
C0042802molecular_functionidentical protein binding
C0044208biological_process'de novo' AMP biosynthetic process
C0044209biological_processAMP salvage
C0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
C0097294biological_process'de novo' XMP biosynthetic process
D0001666biological_processresponse to hypoxia
D0003824molecular_functioncatalytic activity
D0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
D0005829cellular_componentcytosol
D0006164biological_processpurine nucleotide biosynthetic process
D0006167biological_processAMP biosynthetic process
D0006177biological_processGMP biosynthetic process
D0006189biological_process'de novo' IMP biosynthetic process
D0007584biological_processresponse to nutrient
D0009060biological_processaerobic respiration
D0009152biological_processpurine ribonucleotide biosynthetic process
D0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
D0014850biological_processresponse to muscle activity
D0016829molecular_functionlyase activity
D0032991cellular_componentprotein-containing complex
D0042594biological_processresponse to starvation
D0042802molecular_functionidentical protein binding
D0044208biological_process'de novo' AMP biosynthetic process
D0044209biological_processAMP salvage
D0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
D0097294biological_process'de novo' XMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE AMP A 1000
ChainResidue
AARG85
AARG338
AFUM1001
ACL2001
AHOH2054
AHOH2251
AHOH2252
AHOH2253
BHIS159
DARG20
DTYR21
AHIS86
DMET299
DARG303
AASP87
ASER112
AGLN241
AARG329
ALEU331
ASER334
AALA335

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE FUM A 1001
ChainResidue
AHIS86
AMET89
ATHR111
ASER112
AGLN241
AAMP1000
AHOH2255
AHOH2256
BTHR158
BHIS159
DLYS295

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1003
ChainResidue
ALYS35
ATRP39
AASP87
AGLY116
AASP120
ASER334
AARG338
AHOH2161
AHOH2257

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 2001
ChainResidue
AAMP1000
DASN297
DMET299

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 2002
ChainResidue
ATHR111
ATYR114
AARG196
ALYS199
AGLY200

site_idAC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 2SA B 1002
ChainResidue
ATHR158
AHIS159
BARG85
BHIS86
BASP87
BTHR111
BSER112
BGLN241
BARG329
BSER334
BALA335
BARG338
BCL2001
BHOH2038
BHOH2051
BHOH2130
BHOH2161
BHOH2163
BHOH2165
BHOH2166
CARG20
CTYR21
CLYS295
CMET299
CARG303

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1003
ChainResidue
BLYS35
BASP87
BGLY116
BASP120
BSER334
BARG338
BHOH2168

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1004
ChainResidue
BASP120
BARG337
BARG338
BLEU341
BALA342
BHOH2131

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 2001
ChainResidue
B2SA1002
BHOH2166
CASN297

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 2002
ChainResidue
BTHR111
BTYR114
BARG196
BLYS199
BGLY200

site_idBC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AMP C 1000
ChainResidue
CARG85
CHIS86
CASP87
CSER112
CGLN241
CARG329
CLEU331
CSER334
CALA335
CARG338
CFUM1001
CHOH2241
CHOH2242
CHOH2243
DHIS159
BARG20
BTYR21
BMET299
BARG303

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FUM C 1001
ChainResidue
BLYS295
BASN297
CHIS86
CTHR111
CSER112
CGLN241
CAMP1000
DTHR158
DHIS159

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 1003
ChainResidue
CLYS35
CTRP39
CASP87
CGLY116
CASP120
CSER334
CARG338
CHOH2167
CHOH2245

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 2002
ChainResidue
CTYR114
CARG196
CLYS199
CGLY200

site_idBC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 2SA D 1002
ChainResidue
AARG20
ATYR21
ALYS295
AMET299
AARG303
CTHR158
CHIS159
DARG85
DHIS86
DASP87
DTHR111
DSER112
DGLN241
DARG329
DSER334
DALA335
DARG338
DCL2001
DHOH2067
DHOH2087
DHOH2244
DHOH2245
DHOH2246
DHOH2247
DHOH2249

site_idBC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL D 1003
ChainResidue
DLYS35
DTRP39
DASP87
DGLY116
DASP120
DSER334
DARG338
DHOH2212
DHOH2213
DHOH2250

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL D 2001
ChainResidue
AASN297
AMET299
D2SA1002
DHOH2026

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL D 2002
ChainResidue
DTHR111
DTYR114
DARG196
DLYS199
DGLY200

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsaMpYKrN
ChainResidueDetails
AGLY288-ASN297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:22812634
ChainResidueDetails
AHIS159
ASER289
BHIS159
BSER289
CHIS159
CSER289
DHIS159
DSER289

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AARG20
AARG303
BARG20
BARG303
CARG20
CARG303
DARG20
DARG303

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: in other chain
ChainResidueDetails
AARG85
BARG329
BSER334
BARG338
CARG85
CTHR111
CGLN241
CARG329
CSER334
CARG338
DARG85
ATHR111
DTHR111
DGLN241
DARG329
DSER334
DARG338
AGLN241
AARG329
ASER334
AARG338
BARG85
BTHR111
BGLN241

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.8
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS147
ALYS295
BLYS147
BLYS295
CLYS147
CLYS295
DLYS147
DLYS295

site_idSWS_FT_FI6
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS415
BLYS415
CLYS415
DLYS415

218853

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