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3W1J

Crystal structure of the N-terminal truncated selenocysteine synthase SelA in complex with thiosulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0001514biological_processselenocysteine incorporation
A0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
A0005737cellular_componentcytoplasm
B0001514biological_processselenocysteine incorporation
B0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
B0005737cellular_componentcytoplasm
C0001514biological_processselenocysteine incorporation
C0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
C0005737cellular_componentcytoplasm
D0001514biological_processselenocysteine incorporation
D0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
D0005737cellular_componentcytoplasm
E0001514biological_processselenocysteine incorporation
E0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
E0005737cellular_componentcytoplasm
F0001514biological_processselenocysteine incorporation
F0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
F0005737cellular_componentcytoplasm
G0001514biological_processselenocysteine incorporation
G0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
G0005737cellular_componentcytoplasm
H0001514biological_processselenocysteine incorporation
H0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
H0005737cellular_componentcytoplasm
I0001514biological_processselenocysteine incorporation
I0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
I0005737cellular_componentcytoplasm
J0001514biological_processselenocysteine incorporation
J0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
J0005737cellular_componentcytoplasm
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 2001
ChainResidue
AASN140
AASP317
BASN140
BASP317

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE THJ A 2002
ChainResidue
BARG312
BARG315
ATHR82
AARG86
AILE169
AGLY170
BGLU108

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE THJ A 2003
ChainResidue
ATHR76
AASN81
AASN83
BTYR109

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE THJ A 2004
ChainResidue
AILE80
AASN81
ATHR82
AGLY382
AGLY383
JPHE224

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE THJ B 501
ChainResidue
ATYR109
BTHR76
BASN81
BASN83
BVAL419

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE THJ C 501
ChainResidue
CTHR82
CGLY170
DGLU108
DARG312
DARG315

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K D 501
ChainResidue
CASN140
DASN140

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE THJ D 502
ChainResidue
CGLU108
CARG312
CARG315
DTHR82
DILE169
DGLY170

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE THJ D 503
ChainResidue
CTYR109
DASN81
DASN83
DLEU84
DVAL419

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K E 501
ChainResidue
EASN140
EASP317
FASN140
FASP317

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE THJ E 502
ChainResidue
ETHR82
EARG86
EILE169
EGLY170
FGLU108
FARG312
FARG315

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE THJ E 503
ChainResidue
EASN81
EASN83
ELEU84
ETHJ504
FTYR109

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE THJ E 504
ChainResidue
DPHE224
EASN81
ETHR82
EGLY382
ETHJ503

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K G 501
ChainResidue
GASN140
GASP317
HASN140
HASP317

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE THJ H 501
ChainResidue
GTYR109
HTHR76
HASN81
HASN83
HLEU84
HVAL419

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K I 501
ChainResidue
IASN140
IASP317
JASN140
JASP317

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE THJ I 502
ChainResidue
ITHR82
IARG86
IILE169
IGLY170
JGLU108
JARG312
JARG315

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE THJ I 503
ChainResidue
IASN81
IASN83
JTYR109

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE THJ J 501
ChainResidue
IGLU108
IARG312
IARG315
JTHR82
JARG86
JILE169
JGLY170
JGLY171

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE THJ J 502
ChainResidue
JASN81
JASN83
JLEU84
JTHJ503
ITYR109
JTHR76

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE THJ J 503
ChainResidue
APHE224
JVAL78
JILE80
JASN81
JTHR82
JGLY382
JTHJ502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00423
ChainResidueDetails
ALLP285
JLLP285
BLLP285
CLLP285
DLLP285
ELLP285
FLLP285
GLLP285
HLLP285
ILLP285

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PDB entries from 2024-09-11

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