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1MVL

PPC decarboxylase mutant C175S

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
A0015937biological_processcoenzyme A biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0042538biological_processhyperosmotic salinity response
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN A 1001
ChainResidue
ASER27
ASER106
AALA107
AASN108
ATHR109
ACYS118
AASP119
AALA140
AMET141
AHOH1004
AHOH1007
AGLY28
AHOH1015
AHOH1029
AHOH1066
AHOH1097
AHOH1139
ASER29
AVAL30
ATHR53
ASER55
APHE59
ATRP78
ATRP81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11279129, ECO:0000269|PubMed:12614618, ECO:0007744|PDB:1MVN
ChainResidueDetails
AHIS90

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:12614618, ECO:0007744|PDB:1MVN
ChainResidueDetails
ASER175

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10986463, ECO:0000269|PubMed:12614618, ECO:0007744|PDB:1E20, ECO:0007744|PDB:1MVL
ChainResidueDetails
AGLY28
ATHR53
ASER106
AALA140

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:12614618, ECO:0007744|PDB:1MVN
ChainResidueDetails
AASN142
AARG172
AALA174
AMET183

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000305|PubMed:12614618, ECO:0007744|PDB:1MVN
ChainResidueDetails
ASER175

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1mvn
ChainResidueDetails
AHIS90

site_idMCSA1
Number of Residues2
DetailsM-CSA 639
ChainResidueDetails
AHIS90electrostatic stabiliser, proton acceptor
ASER175proton donor

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PDB entries from 2024-07-24

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