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4IFB

Crystal structure of SULT 2A1 LLGG mutant with PAPS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004027molecular_functionalcohol sulfotransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006068biological_processethanol catabolic process
A0006805biological_processxenobiotic metabolic process
A0008146molecular_functionsulfotransferase activity
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0016042biological_processlipid catabolic process
A0016740molecular_functiontransferase activity
A0030573biological_processbile acid catabolic process
A0042403biological_processthyroid hormone metabolic process
A0047704molecular_functionbile-salt sulfotransferase activity
A0050294molecular_functionsteroid sulfotransferase activity
A0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
A0050656molecular_function3'-phosphoadenosine 5'-phosphosulfate binding
A0051923biological_processsulfation
B0004027molecular_functionalcohol sulfotransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006068biological_processethanol catabolic process
B0006805biological_processxenobiotic metabolic process
B0008146molecular_functionsulfotransferase activity
B0008202biological_processsteroid metabolic process
B0008203biological_processcholesterol metabolic process
B0016042biological_processlipid catabolic process
B0016740molecular_functiontransferase activity
B0030573biological_processbile acid catabolic process
B0042403biological_processthyroid hormone metabolic process
B0047704molecular_functionbile-salt sulfotransferase activity
B0050294molecular_functionsteroid sulfotransferase activity
B0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
B0050656molecular_function3'-phosphoadenosine 5'-phosphosulfate binding
B0051923biological_processsulfation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 301
ChainResidue
ALYS248
AASP253
AHIS257

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE PPS A 302
ChainResidue
ATRP49
AHIS99
AARG121
ASER129
ATYR184
ASER218
ASER219
APHE220
AMET223
ALEU245
ALEU246
AARG247
ALYS248
AGLY249
AHOH402
AHOH403
AHOH422
AHOH438
AHOH503
APRO43
ALYS44
ASER45
AGLY46
ATHR47
AASN48

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 303
ChainResidue
AARG174
AGLU176
APHE179
AHOH496
AHOH497

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 301
ChainResidue
BLYS248
BASP253
BASN256
BHIS257

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE PPS B 302
ChainResidue
BPRO43
BLYS44
BSER45
BGLY46
BTHR47
BASN48
BTRP49
BHIS99
BARG121
BSER129
BTYR184
BSER218
BSER219
BPHE220
BMET223
BLEU245
BLEU246
BARG247
BLYS248
BGLY249
BHOH403
BHOH427
BHOH432
BHOH449
BHOH493

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 303
ChainResidue
BHIS58
BLYS60
BLYS204
BHOH477

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 304
ChainResidue
BARG174
BGLU176
BPHE179
BHOH418
BHOH483

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 305
ChainResidue
BTYR131
BPHE132
BHIS257
BHOH410

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11988089, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1J99, ECO:0007744|PDB:1OV4
ChainResidueDetails
AHIS99
BHIS99

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
ChainResidueDetails
ALYS44
AGLY46
AASN48
BLYS44
BGLY46
BASN48

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
ChainResidueDetails
ASER45
BSER45
BTHR47
BTRP49
BARG121
BSER129
BSER218
BARG247
BLYS248
BGLY249
ATHR47
ATRP49
AARG121
ASER129
ASER218
AARG247
ALYS248
AGLY249

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:4IFB
ChainResidueDetails
ATYR184
BTYR184

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:4IFB
ChainResidueDetails
AMET223
BMET223

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER251
BSER251

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PDB entries from 2024-05-01

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