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1IBS

PHOSPHORIBOSYLDIPHOSPHATE SYNTHETASE IN COMPLEX WITH CADMIUM IONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0002189cellular_componentribose phosphate diphosphokinase complex
A0004749molecular_functionribose phosphate diphosphokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006015biological_process5-phosphoribose 1-diphosphate biosynthetic process
A0006164biological_processpurine nucleotide biosynthetic process
A0009156biological_processribonucleoside monophosphate biosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0044249biological_processcellular biosynthetic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0002189cellular_componentribose phosphate diphosphokinase complex
B0004749molecular_functionribose phosphate diphosphokinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006015biological_process5-phosphoribose 1-diphosphate biosynthetic process
B0006164biological_processpurine nucleotide biosynthetic process
B0009156biological_processribonucleoside monophosphate biosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0044249biological_processcellular biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1001
ChainResidue
BASP227
BTHR228
BALA229
BGLY230
BTHR231
BHOH1015
BHOH1029
BHOH1035

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
ATHR228
AALA229
AGLY230
ATHR231
AASP227

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1003
ChainResidue
AARG109
BSER52
BARG54
BSER310
BVAL311
BSER312

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
ASER52
AARG54
ASER310
AVAL311
ASER312
AHOH1016
AHOH1018
BARG109

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1005
ChainResidue
AHIS135
AABM1009

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1006
ChainResidue
AASP174
AASP223

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD B 1007
ChainResidue
BHIS135
BABM1010

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD B 1008
ChainResidue
BASP174
BASP223
BHOH1033

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ABM A 1009
ChainResidue
AARG101
AGLN102
AARG104
AHIS135
ACD1005
AHOH1030
BPHE40
BASP42
BGLU44

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ABM B 1010
ChainResidue
APHE40
AASP42
AGLU44
AGLN46
BARG101
BGLN102
BARG104
BHIS135
BCD1007

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. AILIDDIIDTAgT
ChainResidueDetails
AALA219-THR231

site_idPS00114
Number of Residues16
DetailsPRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHApQIQGFFdiPID
ChainResidueDetails
AASP133-ASP148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:16008562
ChainResidueDetails
ALYS197
BLYS197

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:10742175
ChainResidueDetails
AASP42
BASP42

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:11790837, ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU, ECO:0007744|PDB:1IBS
ChainResidueDetails
AARG101
BARG101

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
ChainResidueDetails
ALYS105
BSER310
AARG109
AGLN140
AASP148
ASER310
BLYS105
BARG109
BGLN140
BASP148

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS
ChainResidueDetails
AHIS135
AASP174
BHIS135
BASP174

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-Rule:MF_00583
ChainResidueDetails
AARG199
AASP223
BARG199
BASP223

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10742175, ECO:0000269|PubMed:11790837, ECO:0007744|PDB:1DKR, ECO:0007744|PDB:1IBS
ChainResidueDetails
AASP227
BASP227

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
AASP224
AASP223
AASP227
ACYS250

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
BASP224
BASP223
BASP227
BCYS250

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PDB entries from 2024-07-10

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