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

5XT6

A sulfur-transferring catalytic intermediate of SufS-SufU complex from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0006534biological_processcysteine metabolic process
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0031071molecular_functioncysteine desulfurase activity
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0006534biological_processcysteine metabolic process
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0031071molecular_functioncysteine desulfurase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006879biological_processintracellular iron ion homeostasis
C0008198molecular_functionferrous iron binding
C0016226biological_processiron-sulfur cluster assembly
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006879biological_processintracellular iron ion homeostasis
D0008198molecular_functionferrous iron binding
D0016226biological_processiron-sulfur cluster assembly
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN D 201
ChainResidue
BHIS342
DASP43
DCYS66
DCYS128

site_idAC2
Number of Residues17
Detailsbinding site for residue PDA A 501
ChainResidue
AASN173
AASP198
AALA200
AGLN201
ASER221
AHIS223
ALYS224
AARG356
AHIS360
AARG376
BGLY274
BTHR275
AALA28
AALA29
ATHR92
ATHR93
AHIS121

site_idAC3
Number of Residues16
Detailsbinding site for residue PDA B 501
ChainResidue
AARG54
AGLY274
ATHR275
BALA28
BTHR92
BTHR93
BHIS121
BASN173
BASP198
BALA200
BGLN201
BSER221
BHIS223
BLYS224
BARG356
BARG376

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN C 201
ChainResidue
AHIS342
CASP43
CCYS66
CCYS128

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. CDFFalSSHKmcgpt.GvGvL
ChainResidueDetails
ACYS215-LEU234

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29235855, ECO:0000269|Ref.10, ECO:0000269|Ref.9
ChainResidueDetails
CCSS41
CASP43
CCYS66
CCYS128

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:31587510, ECO:0007744|PDB:5J8Q
ChainResidueDetails
ALYS224
BLYS224

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon