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4ZDO

The crystal structure of T325S mutant of human SepSecS in complex with selenocysteine tRNA (tRNASec)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0001514biological_processselenocysteine incorporation
A0001717biological_processconversion of seryl-tRNAsec to selenocys-tRNAsec
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0016740molecular_functiontransferase activity
A0098621molecular_functionO-phosphoseryl-tRNA(Sec) selenium transferase activity
B0000049molecular_functiontRNA binding
B0001514biological_processselenocysteine incorporation
B0001717biological_processconversion of seryl-tRNAsec to selenocys-tRNAsec
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0016740molecular_functiontransferase activity
B0098621molecular_functionO-phosphoseryl-tRNA(Sec) selenium transferase activity
C0000049molecular_functiontRNA binding
C0001514biological_processselenocysteine incorporation
C0001717biological_processconversion of seryl-tRNAsec to selenocys-tRNAsec
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0016740molecular_functiontransferase activity
C0098621molecular_functionO-phosphoseryl-tRNA(Sec) selenium transferase activity
D0000049molecular_functiontRNA binding
D0001514biological_processselenocysteine incorporation
D0001717biological_processconversion of seryl-tRNAsec to selenocys-tRNAsec
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0016740molecular_functiontransferase activity
D0098621molecular_functionO-phosphoseryl-tRNA(Sec) selenium transferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue PLR A 1001
ChainResidue
AARG75
ATYR255
ALYS284
APRO311
AGLY312
AARG313
AHOH1102
AHOH1134
AALA143
ATHR144
AGLY145
AILE170
AGLN172
ASER174
AASN252
AALA254

site_idAC2
Number of Residues4
Detailsbinding site for residue PO4 A 1002
ChainResidue
AARG97
ASER98
AGLN105
AHOH1166

site_idAC3
Number of Residues14
Detailsbinding site for residue PLR B 1001
ChainResidue
BARG75
BSER98
BALA143
BTHR144
BGLY145
BGLN172
BSER174
BCYS175
BASN252
BALA254
BTYR255
BLYS284
BGLY312
BARG313

site_idAC4
Number of Residues6
Detailsbinding site for residue PO4 B 1002
ChainResidue
BARG97
BSER98
BGLN105
BARG313
BHOH1101
BHOH1152

site_idAC5
Number of Residues3
Detailsbinding site for residue PO4 C 1002
ChainResidue
CARG97
CGLN105
CHOH1113

site_idAC6
Number of Residues4
Detailsbinding site for residue PO4 D 1002
ChainResidue
DARG97
DGLN105
DARG313
DHOH1122

site_idAC7
Number of Residues20
Detailsbinding site for Di-peptide PLR C 1001 and LYS C 284
ChainResidue
CARG75
CSER98
CALA143
CTHR144
CGLY145
CILE170
CGLN172
CSER174
CASN252
CALA254
CTYR255
CSER281
CLEU282
CASP283
CASN285
CPHE286
CGLY312
CARG313
CILE440
CHOH1122

site_idAC8
Number of Residues22
Detailsbinding site for Di-peptide PLR D 1001 and LYS D 284
ChainResidue
DGLU74
DARG75
DSER98
DALA143
DTHR144
DGLY145
DILE170
DGLN172
DSER174
DASN252
DALA254
DTYR255
DSER281
DLEU282
DASP283
DASN285
DPHE286
DGLY312
DARG313
DILE440
DHOH1117
DHOH1137

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIIKLAGVHTV
ChainResidueDetails
AASP124-VAL134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:19608919
ChainResidueDetails
AARG271
AARG313
AARG398
ALYS463
BARG75
BARG97
BSER98
BGLN105
BARG271
BARG313
BARG398
BLYS463
CARG75
CARG97
CSER98
CGLN105
CARG271
CARG313
CARG398
CLYS463
DARG75
DARG97
DSER98
DGLN105
DARG271
DARG313
DARG398
DLYS463
AARG75
AARG97
ASER98
AGLN105

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate => ECO:0000250|UniProtKB:Q6P6M7
ChainResidueDetails
AGLU74
BGLU74
CGLU74
DGLU74

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER14
BSER14
CSER14
DSER14

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19608919
ChainResidueDetails
ALYS284
BLYS284
CLYS284
DLYS284

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PDB entries from 2024-06-12

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