Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3AP3

Crystal structure of human tyrosylprotein sulfotransferase-2 complexed with PAP

Functional Information from GO Data
ChainGOidnamespacecontents
A0006478biological_processpeptidyl-tyrosine sulfation
A0008476molecular_functionprotein-tyrosine sulfotransferase activity
B0006478biological_processpeptidyl-tyrosine sulfation
B0008476molecular_functionprotein-tyrosine sulfotransferase activity
C0006478biological_processpeptidyl-tyrosine sulfation
C0008476molecular_functionprotein-tyrosine sulfotransferase activity
D0006478biological_processpeptidyl-tyrosine sulfation
D0008476molecular_functionprotein-tyrosine sulfotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE A3P A 1
ChainResidue
AARG78
ATYR238
ASER285
AGLN288
AVAL289
ALYS291
APRO292
AVAL293
AASN294
AALA297
ALYS300
ASER79
AGLY80
ATHR81
ATHR82
ALEU83
AARG183
ASER191
AARG195

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE A3P B 1
ChainResidue
BARG78
BSER79
BGLY80
BTHR81
BTHR82
BARG183
BSER191
BARG195
BTYR238
BVAL289
BLYS291
BPRO292
BASN294
BALA297
BLYS300

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE A3P C 1
ChainResidue
CPRO77
CARG78
CSER79
CGLY80
CTHR81
CTHR82
CARG183
CSER191
CARG195
CTYR238
CSER285
CGLN288
CVAL289
CLYS291
CPRO292
CVAL293
CASN294
CALA297
CLYS300

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE A3P D 1
ChainResidue
DARG78
DSER79
DGLY80
DTHR81
DTHR82
DLEU83
DARG183
DSER191
DARG195
DTYR238
DSER285
DGLN288
DVAL289
DLYS291
DPRO292
DASN294
DALA297
DLYS300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsRegion: {"description":"Interaction with peptide substrate","evidences":[{"source":"PubMed","id":"23481380","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23481380","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues43
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3AP1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AP2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AP3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23481380","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3AP1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AP2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AP3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"23481380","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon