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3GUZ

Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004592molecular_functionpantoate-beta-alanine ligase activity
A0009058biological_processbiosynthetic process
A0015940biological_processpantothenate biosynthetic process
B0003824molecular_functioncatalytic activity
B0004592molecular_functionpantoate-beta-alanine ligase activity
B0009058biological_processbiosynthetic process
B0015940biological_processpantothenate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PAF A 177
ChainResidue
APRO28
AHOH370
ATHR29
AMET30
AGLN61
AILE133
AGLN155
AHOH185
AHOH262
AHOH300

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PAF A 178
ChainResidue
AGLY36
ALYS39
AGLY149
ALYS151
AHOH221
AHOH262
AHOH327
AHOH339
AHOH374

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PAF B 177
ChainResidue
BPRO28
BTHR29
BGLN61
BILE133
BGLN155
BHOH214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS37
BHIS37

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AMET30
AGLN61
AGLY149
AGLN155
BMET30
BGLN61
BGLY149
BGLN155

229183

PDB entries from 2024-12-18

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