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5FT6

Crystal structure of the cysteine desulfurase CsdA (S-sulfonic acid) from Escherichia coli at 2.050 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 Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AALA47
ATHR62
AHOH2439

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AGOL505
AHOH2205
AGLY109
AGLY134
ALYS136
APRO316
AASP393
AGLU397

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AARG60
AARG64
ALYS71
AGLU287

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
AASP310
AALA313
AHOH2349

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
ALYS136
ALYS314
AARG315
AGOL502
AHOH2196
AHOH2355

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 506
ChainResidue
ATYR65
AARG69
ATRP86
AHOH2111
AHOH2112
AHOH2116

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 507
ChainResidue
AMET1
AILE157
ATHR158
APRO159
AALA189

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 1222
ChainResidue
ATHR90
ATHR91
AHIS119
AASN171
AASP196
AALA198
AGLN199
ASER219
AHIS221
ALYS222
AHOH2140
AHOH2143
AHOH2441
BTHR273

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 501
ChainResidue
BTYR65
BARG69
BTRP86
BTRP267
BHOH2068
BHOH2247

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
AHOH2436
BLEU307
BLYS382
BASP386
BVAL389
BHOH2212
BHOH2248

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 503
ChainResidue
BTHR273
BVAL276
BHOH2249
BHOH2250
BHOH2251

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 504
ChainResidue
AHOH2385
BTHR306
BGLU309
BASP310
BASP325

site_idBC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 1222
ChainResidue
ATHR273
AHOH2315
AHOH2316
AHOH2319
BTHR90
BTHR91
BHIS119
BASN171
BASP196
BALA198
BGLN199
BSER219
BHIS221
BLYS222
BHOH2088

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
ACSU358
BCSU358

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

220113

PDB entries from 2024-05-22

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