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3MXT

Crystal Structure of Pantoate-Beta-alanine Ligase from Campylobacter jejuni

Functional Information from GO Data
ChainGOidnamespacecontents
A0004592molecular_functionpantoate-beta-alanine ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0015940biological_processpantothenate biosynthetic process
A0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 287
ChainResidue
AGLN60
AVAL130
AGLN152
AFMT296
AHOH542
AHOH594

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 288
ChainResidue
AHOH534
AHOH589
AHOH652
AASN139
AASP166
AHOH414

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 289
ChainResidue
AHIS34
AARG76
ASER184
ASER185
AFMT292
AHOH300
AHOH507

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 290
ChainResidue
AMSE30
AGLN60
AARG120
AHIS123
AARG186
AHOH487

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 291
ChainResidue
APRO28
AHIS34
AHIS37
ALEU40
AGLY146
ALYS148
AFMT296
AHOH317
AHOH318
AHOH319

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 292
ChainResidue
AHIS34
AASP35
ALYS183
ASO4289
AHOH524

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 295
ChainResidue
AHIS34
ASER184
ASER185

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 296
ChainResidue
ATHR29
AMSE30
AHIS37
AGOL287
AGOL291
AHOH348
AHOH383

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00158
ChainResidueDetails
AHIS37

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00158
ChainResidueDetails
AMSE30
AGLN60
AGLY146
AGLN152
AILE175
ALYS183

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PDB entries from 2024-10-09

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