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1J1Z

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0000053biological_processargininosuccinate metabolic process
A0000166molecular_functionnucleotide binding
A0004055molecular_functionargininosuccinate synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006526biological_processL-arginine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016874molecular_functionligase activity
B0000050biological_processurea cycle
B0000053biological_processargininosuccinate metabolic process
B0000166molecular_functionnucleotide binding
B0004055molecular_functionargininosuccinate synthase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006526biological_processL-arginine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0016874molecular_functionligase activity
C0000050biological_processurea cycle
C0000053biological_processargininosuccinate metabolic process
C0000166molecular_functionnucleotide binding
C0004055molecular_functionargininosuccinate synthase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006526biological_processL-arginine biosynthetic process
C0008652biological_processamino acid biosynthetic process
C0016874molecular_functionligase activity
D0000050biological_processurea cycle
D0000053biological_processargininosuccinate metabolic process
D0000166molecular_functionnucleotide binding
D0004055molecular_functionargininosuccinate synthase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006526biological_processL-arginine biosynthetic process
D0008652biological_processamino acid biosynthetic process
D0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 510
ChainResidue
AALA6
AHIS113
AGLY114
APHE125
ASER173
AASP175
ACIR520
AASP530
ASER8
AASP12
ATHR13
APHE31
ATHR32
AALA33
AGLN37
AARG92

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP B 2510
ChainResidue
AASP2530
BALA6
BTYR7
BSER8
BGLY10
BASP12
BTHR13
BPHE31
BTHR32
BALA33
BGLN37
BARG92
BHIS113
BGLY114
BPHE125
BHOH1506

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP C 3510
ChainResidue
AASP3530
CALA6
CSER8
CASP12
CTHR13
CPHE31
CTHR32
CALA33
CGLN37
CARG92
CILE95
CHIS113
CGLY114
CALA115
CPHE125
CSER173
CASP175
CHOH1541
CCIR3520

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP D 4510
ChainResidue
AASP4530
DALA6
DTYR7
DSER8
DGLY10
DLEU11
DASP12
DTHR13
DPHE31
DALA33
DGLN37
DARG92
DHIS113
DGLY114
DPHE125
DHOH1479
DCIR4520

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CIR A 520
ChainResidue
ATYR84
ATHR88
ASER89
AASN120
AARG124
ASER173
AMET174
ASER182
AGLU184
AGLU258
ATYR270
ATYR310
AATP510
AASP530
AHOH1017

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CIR B 2520
ChainResidue
AASP2530
BTYR84
BTHR88
BSER89
BASN120
BARG124
BSER173
BMET174
BASP175
BSER182
BGLU184
BGLU258
BTYR270
BTYR310
BHOH1039

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CIR C 3520
ChainResidue
CTYR84
CTHR88
CSER89
CASN120
CASP121
CARG124
CSER173
CMET174
CSER182
CGLU184
CGLU258
CTYR270
CTYR310
CATP3510
AASP3530

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CIR D 4520
ChainResidue
AHOH1124
AASP4530
DTYR84
DTHR88
DSER89
DASN120
DARG124
DSER173
DMET174
DASP175
DSER182
DGLU184
DGLU258
DTYR270
DTYR310
DATP4510

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ASP A 530
ChainResidue
AALA115
ATHR116
AGLY119
AASN120
AASP121
AATP510
ACIR520
AHOH1017
AHOH1071
AHOH1159

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ASP A 2530
ChainResidue
AHOH1049
BALA115
BTHR116
BGLY119
BASN120
BASP121
BHOH1039
BHOH1099
BATP2510
BCIR2520

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ASP A 3530
ChainResidue
AHOH1004
AHOH1117
CALA115
CTHR116
CGLY119
CASN120
CASP121
CHOH1028
CATP3510
CCIR3520

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ASP A 4530
ChainResidue
AHOH1124
AHOH1161
DALA115
DTHR116
DGLY119
DASN120
DASP121
DGLU184
DHOH1212
DATP4510
DCIR4520

Functional Information from PROSITE/UniProt
site_idPS00564
Number of Residues9
DetailsARGININOSUCCIN_SYN_1 Argininosuccinate synthase signature 1. AYSGGLDTS
ChainResidueDetails
AALA6-SER14

site_idPS00565
Number of Residues12
DetailsARGININOSUCCIN_SYN_2 Argininosuccinate synthase signature 2. GaTgKGNDqvRF
ChainResidueDetails
AGLY114-PHE125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00005","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11844799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12684518","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
AASP121
AARG92

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
BASP121
BARG92

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
CASP121
CARG92

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
DASP121
DARG92

site_idMCSA1
Number of Residues4
DetailsM-CSA 316
ChainResidueDetails
AASP12steric role
AARG92electrostatic stabiliser, hydrogen bond donor
AASP121proton acceptor, proton donor
ASER173hydrogen bond donor, steric role

site_idMCSA2
Number of Residues4
DetailsM-CSA 316
ChainResidueDetails
BASP12steric role
BARG92electrostatic stabiliser, hydrogen bond donor
BASP121proton acceptor, proton donor
BSER173hydrogen bond donor, steric role

site_idMCSA3
Number of Residues4
DetailsM-CSA 316
ChainResidueDetails
CASP12steric role
CARG92electrostatic stabiliser, hydrogen bond donor
CASP121proton acceptor, proton donor
CSER173hydrogen bond donor, steric role

site_idMCSA4
Number of Residues4
DetailsM-CSA 316
ChainResidueDetails
DASP12steric role
DARG92electrostatic stabiliser, hydrogen bond donor
DASP121proton acceptor, proton donor
DSER173hydrogen bond donor, steric role

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PDB entries from 2025-10-08

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