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3HL2

The crystal structure of the human SepSecS-tRNASec complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0001514biological_processselenocysteine incorporation
A0001717biological_processconversion of seryl-tRNAsec to selenocys-tRNAsec
A0003723molecular_functionRNA binding
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
B0003723molecular_functionRNA binding
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
C0003723molecular_functionRNA binding
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
D0003723molecular_functionRNA binding
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 Residues17
DetailsBINDING SITE FOR RESIDUE PLR A 1001
ChainResidue
AGLU74
AASN252
AALA254
ATYR255
ALYS284
AGLY312
AARG313
AHOH525
AHOH564
AARG75
AALA143
ATHR144
AGLY145
AILE170
AGLN172
ASER174
ACYS175

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TS6 A 3001
ChainResidue
AARG97
ASER98
AGLN105

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TS6 A 3002
ChainResidue
AARG199
AHIS368

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLR B 1001
ChainResidue
BARG75
BALA143
BTHR144
BGLY145
BILE170
BGLN172
BSER174
BASN252
BALA254
BTYR255
BLYS284
BPRO311
BGLY312
BARG313
BHOH570
BSEP2001

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SEP B 2001
ChainResidue
BGLU74
BARG75
BARG97
BSER98
BGLY99
BGLN105
BGLN172
BLYS173
BPHE227
BLYS284
BARG313
BHOH570
BPLR1001

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SEP B 2002
ChainResidue
BARG199
BARG234
BHIS368

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLR C 1001
ChainResidue
CARG75
CALA143
CTHR144
CGLY145
CILE170
CGLN172
CSER174
CCYS175
CASN252
CALA254
CTYR255
CLYS284
CGLY312
CARG313

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TS6 C 3001
ChainResidue
CARG97
CSER98
CGLN105

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLR D 1001
ChainResidue
DARG75
DALA143
DTHR144
DGLY145
DGLN172
DSER174
DCYS175
DASN252
DALA254
DTYR255
DLYS284
DGLY312
DARG313
DSEP2001

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SEP D 2001
ChainResidue
DGLU74
DARG75
DARG97
DSER98
DGLY99
DGLN105
DGLN172
DLYS173
DLYS284
DARG313
DPLR1001

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SEP D 2002
ChainResidue
DHOH535
DARG199
DARG234
DHIS368

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 Residues40
DetailsRegion: {"description":"Phosphate loop (P-loop)","evidences":[{"source":"PubMed","id":"19608919","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19608919","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate","evidences":[{"source":"UniProtKB","id":"Q6P6M7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"19608919","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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