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1U80

Phosphopantothenoylcysteine synthetase from E. coli, CMP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004632molecular_functionphosphopantothenate--cysteine ligase activity
A0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
A0010181molecular_functionFMN binding
A0015937biological_processcoenzyme A biosynthetic process
A0015941biological_processpantothenate catabolic process
B0004632molecular_functionphosphopantothenate--cysteine ligase activity
B0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
B0010181molecular_functionFMN binding
B0015937biological_processcoenzyme A biosynthetic process
B0015941biological_processpantothenate catabolic process
C0004632molecular_functionphosphopantothenate--cysteine ligase activity
C0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
C0010181molecular_functionFMN binding
C0015937biological_processcoenzyme A biosynthetic process
C0015941biological_processpantothenate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AHOH38
ASER212
ASER213
AGLY214
ALYS215
AMET216
APHE362
AASN363
ALYS385

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 1501
ChainResidue
BSER212
BSER213
BGLY214
BLYS215
BMET216
BPHE362
BASN363
BLYS385

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 C 2501
ChainResidue
CSER212
CSER213
CGLY214
CLYS215
CMET216
CPHE362
CASN363
CLYS385

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE C5P A 500
ChainResidue
AHOH32
AGLY273
AALA275
AVAL277
APRO308
AASP309
AILE310
AVAL311
AGLY326
APHE327
ALYS341
ALYS345
BLYS289

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE C5P B 1500
ChainResidue
ALYS289
ALYS292
BGLY273
BALA275
BVAL277
BPRO308
BASP309
BILE310
BVAL311
BGLY326
BPHE327
BLYS341
BLYS345

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE C5P C 2500
ChainResidue
CGLY273
CALA275
CVAL277
CASP279
CLYS289
CPRO308
CASP309
CILE310
CVAL311
CGLY326
CPHE327
CLYS341
CLYS345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W
ChainResidueDetails
ACYS274
BILE290
BASP309
BALA328
BARG342
BASN346
CCYS274
CTYR280
CILE290
CASP309
CALA328
ATYR280
CARG342
CASN346
AILE290
AASP309
AALA328
AARG342
AASN346
BCYS274
BTYR280

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1u7u
ChainResidueDetails
AASP210

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1u7u
ChainResidueDetails
BASP210

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1u7u
ChainResidueDetails
CASP210

site_idMCSA1
Number of Residues1
DetailsM-CSA 772
ChainResidueDetails
AHIS211activator, electrostatic stabiliser

site_idMCSA2
Number of Residues1
DetailsM-CSA 772
ChainResidueDetails
BHIS211activator, electrostatic stabiliser

site_idMCSA3
Number of Residues1
DetailsM-CSA 772
ChainResidueDetails
CHIS211activator, electrostatic stabiliser

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PDB entries from 2024-07-24

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