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3GZC

Structure of human selenocysteine lyase

Replaces:  2HDY
Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0009000molecular_functionselenocysteine lyase activity
A0016261biological_processselenocysteine catabolic process
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0042803molecular_functionprotein homodimerization activity
A0070279molecular_functionvitamin B6 binding
A1902494cellular_componentcatalytic complex
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0009000molecular_functionselenocysteine lyase activity
B0016261biological_processselenocysteine catabolic process
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0016829molecular_functionlyase activity
B0042803molecular_functionprotein homodimerization activity
B0070279molecular_functionvitamin B6 binding
B1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLR A 500
ChainResidue
AGLY99
ALYS259
AHOH461
AHOH470
AHOH596
BTHR296
ATHR100
AHIS145
ASER147
AASP233
AALA235
AGLN236
AVAL256
AHIS258

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLR B 500
ChainResidue
ATHR296
BGLY99
BTHR100
BHIS145
BSER147
BASP233
BALA235
BGLN236
BHIS258
BLYS259
BHOH459
BHOH569
BHOH666

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"S-selanylcysteine intermediate","evidences":[{"source":"UniProtKB","id":"Q68FT9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2006","submissionDatabase":"PDB data bank","title":"Structure of human selenocysteine lyase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
APHE138
AASP233

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BPHE138
BASP233

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
ALYS259
AHIS145
AASP233

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BLYS259
BHIS145
BASP233

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
ACYS388
ALYS259

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BCYS388
BLYS259

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
AARG69

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BARG69

239803

PDB entries from 2025-08-06

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