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5FT5

Crystal structure of the cysteine desulfurase CsdA (persulfurated) from Escherichia coli at 2.384 Angstroem resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000096biological_processsulfur amino acid metabolic process
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0006534biological_processcysteine metabolic process
A0008826molecular_functioncysteine sulfinate desulfinase activity
A0009000molecular_functionselenocysteine lyase activity
A0016226biological_processiron-sulfur cluster assembly
A0016261biological_processselenocysteine catabolic process
A0016740molecular_functiontransferase activity
A0016783molecular_functionsulfurtransferase activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0019448biological_processL-cysteine catabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0031071molecular_functioncysteine desulfurase activity
A0072348biological_processsulfur compound transport
A1990221cellular_componentL-cysteine desulfurase complex
B0000096biological_processsulfur amino acid metabolic process
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0006534biological_processcysteine metabolic process
B0008826molecular_functioncysteine sulfinate desulfinase activity
B0009000molecular_functionselenocysteine lyase activity
B0016226biological_processiron-sulfur cluster assembly
B0016261biological_processselenocysteine catabolic process
B0016740molecular_functiontransferase activity
B0016783molecular_functionsulfurtransferase activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0019448biological_processL-cysteine catabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0031071molecular_functioncysteine desulfurase activity
B0072348biological_processsulfur compound transport
B1990221cellular_componentL-cysteine desulfurase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1402
ChainResidue
ATHR28
BALA47
BTHR273
BVAL276

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1402
ChainResidue
AGOL1406
AARG302
APRO316
AGLN324
AALA334
AVAL400

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1403
ChainResidue
ATYR65
AARG69
ATRP86
AHOH2034
AHOH2035

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1404
ChainResidue
AALA63
AARG64
ALYS71
AGLU287

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1405
ChainResidue
AHIS338
ASER339
AHOH2130

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1406
ChainResidue
AVAL400
AGOL1402
AHOH2116

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1407
ChainResidue
APHE4
ATRP300
AARG319

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 1408
ChainResidue
AARG10
ATRP300
ATHR381
ALYS382
ASER383

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TLA A 1409
ChainResidue
AALA26
AALA27
AHIS119
AASN171
ALYS222
AARG353
AHIS357
ACSS358
AARG373
APLP1410
BLYS250

site_idBC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 1410
ChainResidue
ATHR90
ATHR91
AHIS119
AASN171
AASP196
AALA198
AGLN199
ASER219
AHIS221
ALYS222
ATLA1409
AHOH2043
AHOH2152
BGLY272
BTHR273

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1403
ChainResidue
BTYR65
BGLU66
BALA68
BARG69
BTRP86

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1404
ChainResidue
AASP151
BARG10
BTHR381
BSER383

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1405
ChainResidue
BHIS51
BARG52
BPHE55
BPHE204
BARG302
BGLN324
BHOH2132

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TLA B 1406
ChainResidue
BHIS119
BLYS222
BARG353
BHIS357
BCSS358
BARG373
BPLP1407
BHOH2147

site_idBC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 1407
ChainResidue
AGLY272
ATHR273
BTHR90
BTHR91
BHIS119
BALA121
BASP196
BALA198
BGLN199
BSER219
BHIS221
BLYS222
BTLA1406
BHOH2052
BHOH2147

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDFYafSGHKlygpt.GiGvL
ChainResidueDetails
AILE213-LEU232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Cysteine persulfide intermediate => ECO:0000305|PubMed:10739946
ChainResidueDetails
ACSS358
BCSS358

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS222
BLYS222

219869

PDB entries from 2024-05-15

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