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5A11

The crystal structure of Ta-TFP, a thiocyanate-forming protein involved in glucosinolate breakdown (space group P21)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0016829molecular_functionlyase activity
A0019760biological_processglucosinolate metabolic process
A0030234molecular_functionenzyme regulator activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0080028biological_processnitrile biosynthetic process
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0016829molecular_functionlyase activity
B0019760biological_processglucosinolate metabolic process
B0030234molecular_functionenzyme regulator activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0080028biological_processnitrile biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1349
ChainResidue
AARG157

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 1349
ChainResidue
BARG157

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 1350
ChainResidue
BARG80

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1350
ChainResidue
AARG80

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1351
ChainResidue
AMET10

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 1351
ChainResidue
BARG94
BLYS148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:26260516, ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313
ChainResidueDetails
AARG94
BARG94

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313
ChainResidueDetails
AARG157
BARG157

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:30900313
ChainResidueDetails
AGLU220
BGLU220

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:23999604
ChainResidueDetails
AGLU46
AVAL310
BGLU46
BVAL310

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313
ChainResidueDetails
AARG94
AGLU266
AASP270
AHIS274
BARG94
BGLU266
BASP270
BHIS274

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:28479247
ChainResidueDetails
ATHR129
BTHR129

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:30900313
ChainResidueDetails
APHE130
BPHE130

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313
ChainResidueDetails
AARG157
ATRP309
BARG157
BTRP309

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:28479247
ChainResidueDetails
AARG269
BARG269

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Essential for catalytic activity => ECO:0000269|PubMed:30900313
ChainResidueDetails
ATYR45
BTYR45

site_idSWS_FT_FI11
Number of Residues2
DetailsSITE: Critical for thiocyanate and epithionitrile formation with allylglucosinolate in the presence of myrosinase => ECO:0000269|PubMed:30900313
ChainResidueDetails
ATHR154
BTHR154

224572

PDB entries from 2024-09-04

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