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4ZDL

The crystal structure of the T325S mutant of the human holo SepSecS

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
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue PLR A 1001
ChainResidue
AARG75
AALA254
ATYR255
ALYS284
AGLY312
AARG313
AFLC1002
AHOH1110
AHOH1184
AHOH1219
AHOH1245
ASER98
AALA143
ATHR144
AGLY145
AILE170
AGLN172
ASER174
AASN252

site_idAC2
Number of Residues11
Detailsbinding site for residue FLC A 1002
ChainResidue
AARG75
AARG97
ASER98
AGLN105
ALYS107
AARG313
AARG404
APLR1001
AHOH1112
AHOH1154
AHOH1174

site_idAC3
Number of Residues22
Detailsbinding site for Di-peptide PLR B 1001 and LYS B 284
ChainResidue
BGLU74
BARG75
BALA143
BTHR144
BGLY145
BILE170
BGLN172
BSER174
BASN252
BALA254
BTYR255
BSER281
BLEU282
BASP283
BASN285
BPHE286
BGLY312
BARG313
BILE440
BHOH1110
BHOH1121
BHOH1126

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 Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:19608919
ChainResidueDetails
AARG75
BARG97
BSER98
BGLN105
BARG271
BARG313
BARG398
BLYS463
AARG97
ASER98
AGLN105
AARG271
AARG313
AARG398
ALYS463
BARG75

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate => ECO:0000250|UniProtKB:Q6P6M7
ChainResidueDetails
AGLU74
BGLU74

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER14
BSER14

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19608919
ChainResidueDetails
ALYS284
BLYS284

220113

PDB entries from 2024-05-22

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