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6RS4

Structure of tabersonine synthase - an alpha-beta hydrolase from Catharanthus roseus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0009820biological_processalkaloid metabolic process
A0009821biological_processalkaloid biosynthetic process
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0035834biological_processindole alkaloid metabolic process
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0009820biological_processalkaloid metabolic process
B0009821biological_processalkaloid biosynthetic process
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0035834biological_processindole alkaloid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 401
ChainResidue
AGLY81
ASER170
ATHR171
ATYR204
AHOH505
AHOH697
AHOH733

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 402
ChainResidue
ALYS89
AEDO403
AHOH587
ASER28
AGLU85

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 403
ChainResidue
ATYR31
ASER86
ALYS89
AEDO402
AHOH720
AHOH729
BTYR31

site_idAC4
Number of Residues8
Detailsbinding site for residue EDO A 404
ChainResidue
AHIS137
AVAL138
AGLY139
ALEU140
AILE156
APHE161
AHOH510
AHOH702

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 405
ChainResidue
ALEU206
AILE207
AARG208
AARG222
AASN236
AASP237
AHOH633

site_idAC6
Number of Residues10
Detailsbinding site for residue EDO A 406
ChainResidue
AGLU129
AGLN132
ATRP133
ASER136
ALYS151
AHOH507
AHOH521
AHOH522
AHOH537
AHOH547

site_idAC7
Number of Residues11
Detailsbinding site for residue EDO B 401
ChainResidue
BGLY81
BSER170
BTHR171
BTYR202
BTYR204
BTYR221
BTYR224
BHOH509
BHOH556
BHOH565
BHOH632

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO B 402
ChainResidue
APRO30
ATYR31
AHOH729
BLYS89
BHOH569

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO B 403
ChainResidue
BHIS137
BVAL138
BGLY139
BLEU140
BPHE161
BHOH547
BHOH715

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 404
ChainResidue
BARG25
BSER86
BLYS89
BHOH520
BHOH607

site_idAD2
Number of Residues10
Detailsbinding site for residue EDO B 405
ChainResidue
BGLU129
BGLN132
BTRP133
BSER136
BLYS151
BHOH506
BHOH511
BHOH527
BHOH528
BHOH553

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMotif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"32066966","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"32066966","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"32066966","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A2P1GIW2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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