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1P3W

X-ray crystal structure of E. coli IscS

Functional Information from GO Data
ChainGOidnamespacecontents
A0002143biological_processtRNA wobble position uridine thiolation
A0002937biological_processtRNA 4-thiouridine biosynthesis
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008033biological_processtRNA processing
A0009000molecular_functionselenocysteine lyase activity
A0009228biological_processthiamine biosynthetic process
A0009589biological_processdetection of UV
A0016226biological_processiron-sulfur cluster assembly
A0016261biological_processselenocysteine catabolic process
A0016740molecular_functiontransferase activity
A0018131biological_processoxazole or thiazole biosynthetic process
A0019448biological_processL-cysteine catabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0031071molecular_functioncysteine desulfurase activity
A0044571biological_process[2Fe-2S] cluster assembly
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0072348biological_processsulfur compound transport
A0097163molecular_functionsulfur carrier activity
A1990221cellular_componentL-cysteine desulfurase complex
A1990228cellular_componentsulfurtransferase complex
A1990329cellular_componentIscS-TusA complex
A1990330cellular_componentIscS-IscU complex
B0002143biological_processtRNA wobble position uridine thiolation
B0002937biological_processtRNA 4-thiouridine biosynthesis
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008033biological_processtRNA processing
B0009000molecular_functionselenocysteine lyase activity
B0009228biological_processthiamine biosynthetic process
B0009589biological_processdetection of UV
B0016226biological_processiron-sulfur cluster assembly
B0016261biological_processselenocysteine catabolic process
B0016740molecular_functiontransferase activity
B0018131biological_processoxazole or thiazole biosynthetic process
B0019448biological_processL-cysteine catabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0031071molecular_functioncysteine desulfurase activity
B0044571biological_process[2Fe-2S] cluster assembly
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0072348biological_processsulfur compound transport
B0097163molecular_functionsulfur carrier activity
B1990221cellular_componentL-cysteine desulfurase complex
B1990228cellular_componentsulfurtransferase complex
B1990329cellular_componentIscS-TusA complex
B1990330cellular_componentIscS-IscU complex
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 764
ChainResidue
ATHR243
BGLN183
BSER203
BHIS205
BLYS206
BHOH795
BHOH848
BHOH925
AHOH880
BALA75
BTHR76
BHIS104
BMET151
BASN155
BASP180
BTHR182

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 764
ChainResidue
AALA75
ATHR76
AHIS104
AMET151
AASN155
AASP180
ATHR182
AGLN183
ASER203
AHIS205
ALYS206
AHOH801
AHOH823
AHOH895
BTHR243

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. VDLMsfSGHKiygpk.GiGaL
ChainResidueDetails
BVAL197-LEU216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Cysteine persulfide intermediate => ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:12860127, ECO:0000269|PubMed:8663056
ChainResidueDetails
BCYS328
ACYS328

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00331
ChainResidueDetails
AALA75
AASN155
BALA75
BASN155

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:12860127
ChainResidueDetails
BTHR243
AGLN183
ASER203
ATHR243
BGLN183
BSER203

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: via persulfide group => ECO:0000255|HAMAP-Rule:MF_00331
ChainResidueDetails
BCYS328
ACYS328

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:12860127
ChainResidueDetails
BLYS206
ALYS206

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PDB entries from 2024-04-17

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