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3A9C

Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakaraensis KOD1 in complex with ribulose-1,5-bisphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016853molecular_functionisomerase activity
A0019323biological_processpentose catabolic process
A0019509biological_processL-methionine salvage from methylthioadenosine
A0043917molecular_functionribose 1,5-bisphosphate isomerase activity
A0044237biological_processcellular metabolic process
A0044249biological_processcellular biosynthetic process
A0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
B0016853molecular_functionisomerase activity
B0019323biological_processpentose catabolic process
B0019509biological_processL-methionine salvage from methylthioadenosine
B0043917molecular_functionribose 1,5-bisphosphate isomerase activity
B0044237biological_processcellular metabolic process
B0044249biological_processcellular biosynthetic process
B0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
C0016853molecular_functionisomerase activity
C0019323biological_processpentose catabolic process
C0019509biological_processL-methionine salvage from methylthioadenosine
C0043917molecular_functionribose 1,5-bisphosphate isomerase activity
C0044237biological_processcellular metabolic process
C0044249biological_processcellular biosynthetic process
C0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
D0016853molecular_functionisomerase activity
D0019323biological_processpentose catabolic process
D0019509biological_processL-methionine salvage from methylthioadenosine
D0043917molecular_functionribose 1,5-bisphosphate isomerase activity
D0044237biological_processcellular metabolic process
D0044249biological_processcellular biosynthetic process
D0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
E0016853molecular_functionisomerase activity
E0019323biological_processpentose catabolic process
E0019509biological_processL-methionine salvage from methylthioadenosine
E0043917molecular_functionribose 1,5-bisphosphate isomerase activity
E0044237biological_processcellular metabolic process
E0044249biological_processcellular biosynthetic process
E0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
F0016853molecular_functionisomerase activity
F0019323biological_processpentose catabolic process
F0019509biological_processL-methionine salvage from methylthioadenosine
F0043917molecular_functionribose 1,5-bisphosphate isomerase activity
F0044237biological_processcellular metabolic process
F0044249biological_processcellular biosynthetic process
F0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE RUB A 401
ChainResidue
ACSD133
AHOH601
AHOH614
ASER135
ALYS136
AALA137
AALA201
AASN212
ALYS213
ALYS238
AARG254

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 402
ChainResidue
ALYS224
AVAL228
AGLU285
AASP288

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 411
ChainResidue
AASP304
EASP304

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RUB B 401
ChainResidue
BCSD133
BSER135
BLYS136
BALA137
BALA201
BASP202
BASN212
BLYS213
BLYS238
BARG254
BHOH601
BHOH603
BHOH615

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG B 402
ChainResidue
BALA223
BLYS224
BARG227
BVAL228
BTHR230
BTYR286
BASP288

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 411
ChainResidue
BASP304
DASP304

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE RUB C 401
ChainResidue
CCSD133
CSER135
CLYS136
CALA137
CGLN164
CALA201
CASN212
CLYS213
CLYS238
CARG254
CHOH601
CHOH609

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG C 402
ChainResidue
CLYS224
CVAL228
CGLU285
CTYR286
CASP288

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RUB D 401
ChainResidue
DCSD133
DSER135
DLYS136
DALA137
DGLN164
DALA201
DASN212
DLYS213
DLYS238
DARG254
DHOH601
DHOH620
DHOH627

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG D 402
ChainResidue
DLYS224
DARG227
DVAL228
DTYR286
DASP288
DHOH619

site_idBC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE RUB E 401
ChainResidue
ECSD133
ESER135
ELYS136
EALA137
EGLN164
EALA201
EASN212
ELYS213
ELYS238
EARG254
EHOH601
EHOH618

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG E 402
ChainResidue
ELYS224
EARG227
EVAL228
ETRP229
EASP288

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE RUB F 401
ChainResidue
FLYS238
FARG254
FHOH601
FHOH633
FCSD133
FSER135
FLYS136
FALA137
FLYS162
FASN212
FLYS213

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG F 402
ChainResidue
FLYS224
FARG227
FVAL228
FTHR230
FASP288
FHOH637

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
ChainResidueDetails
ACSD133
BCSD133
CCSD133
DCSD133
ECSD133
FCSD133

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
ChainResidueDetails
AASP202
BASP202
CASP202
DASP202
EASP202
FASP202

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230
ChainResidueDetails
AARG20
DARG20
DSER135
DASN212
EARG20
ESER135
EASN212
FARG20
FSER135
FASN212
ASER135
AASN212
BARG20
BSER135
BASN212
CARG20
CSER135
CASN212

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
ChainResidueDetails
AARG63
ELYS238
FARG63
FLYS238
ALYS238
BARG63
BLYS238
CARG63
CLYS238
DARG63
DLYS238
EARG63

site_idSWS_FT_FI5
Number of Residues6
DetailsSITE: Plays a key role in hexamerization
ChainResidueDetails
AARG227
BARG227
CARG227
DARG227
EARG227
FARG227

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건을2024-09-18부터공개중

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