Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3LVM

Crystal Structure of E.coli IscS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008033biological_processtRNA processing
A0016226biological_processiron-sulfur cluster assembly
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0031071molecular_functioncysteine desulfurase activity
A0044571biological_process[2Fe-2S] cluster assembly
A0046872molecular_functionmetal ion binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008033biological_processtRNA processing
B0016226biological_processiron-sulfur cluster assembly
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0031071molecular_functioncysteine desulfurase activity
B0044571biological_process[2Fe-2S] cluster assembly
B0046872molecular_functionmetal ion binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 764
ChainResidue
AGLY74
ASER203
AHIS205
ALYS206
AHOH426
AHOH528
BTHR243
AALA75
ATHR76
AHIS104
AMET151
AASN155
AASP180
ATHR182
AGLN183

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 764
ChainResidue
ATHR243
BGLY74
BALA75
BTHR76
BHIS104
BMET151
BASN155
BASP180
BTHR182
BGLN183
BSER203
BHIS205
BLYS206
BHOH491
BHOH539

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. VDLMsfSGHKiygpk.GiGaL
ChainResidueDetails
AVAL197-LEU216

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

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:20404999
ChainResidueDetails
AALA75
AGLN183
ASER203
ATHR243
BALA75
BGLN183
BSER203
BTHR243

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00331
ChainResidueDetails
AASN155
BASN155

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

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:20404999
ChainResidueDetails
ALYS206
BLYS206

219515

PDB entries from 2024-05-08

PDB statisticsPDBj update infoContact PDBjnumon