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3A9Z

Crystal structure of ras selenocysteine lyase in complex with selenopropionate

Functional Information from GO Data
ChainGOidnamespacecontents
A0001887biological_processselenium compound metabolic process
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0009000molecular_functionselenocysteine lyase activity
A0016261biological_processselenocysteine catabolic process
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0032868biological_processresponse to insulin
A0042803molecular_functionprotein homodimerization activity
A0070279molecular_functionvitamin B6 binding
A1900408biological_processnegative regulation of cellular response to oxidative stress
A1902494cellular_componentcatalytic complex
B0001887biological_processselenium compound metabolic process
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0009000molecular_functionselenocysteine lyase activity
B0016261biological_processselenocysteine catabolic process
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0016829molecular_functionlyase activity
B0032868biological_processresponse to insulin
B0042803molecular_functionprotein homodimerization activity
B0070279molecular_functionvitamin B6 binding
B1900408biological_processnegative regulation of cellular response to oxidative stress
B1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
AGLY87
ALYS247
AHOH463
AHOH464
AHOH483
ASLP502
BGLY283
BTHR284
ATHR88
AHIS133
AMET182
AASP221
AALA223
AGLN224
AVAL244
AHIS246

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SLP A 502
ChainResidue
AASN25
AALA26
AHIS133
AASN186
ALYS247
AALA373
ASER374
ACYS375
AARG402
APLP501

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 504
ChainResidue
AARG312
AARG315
AARG341
AGLY352
ASER353
AHOH540
AHOH573
AHOH590

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 505
ChainResidue
AHIS310
AASP313
AHOH630

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 501
ChainResidue
AGLY283
ATHR284
BGLY87
BTHR88
BHIS133
BMET182
BASP221
BALA223
BGLN224
BVAL244
BHIS246
BLYS247
BHOH442
BHOH444
BHOH475
BSLP503

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SLP B 503
ChainResidue
BASN25
BALA26
BHIS133
BASN186
BLYS247
BALA373
BSER374
BCYS375
BARG402
BPLP501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: S-selanylcysteine intermediate => ECO:0000269|PubMed:20164179
ChainResidueDetails
ACYS375
BCYS375

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q96I15
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q96I15
ChainResidueDetails
ASER117
BSER117

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20164179, ECO:0007744|PDB:3A9X, ECO:0007744|PDB:3A9Y, ECO:0007744|PDB:3A9Z
ChainResidueDetails
ALYS247
BLYS247

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PDB entries from 2024-06-12

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