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3QTT

Crystal Structure of Pantoate-beta-alanine Ligase from Francisella tularensis Complexed with Beta-gamma ATP and Beta-alanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004592molecular_functionpantoate-beta-alanine ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0015940biological_processpantothenate biosynthetic process
A0016874molecular_functionligase activity
B0003824molecular_functioncatalytic activity
B0004592molecular_functionpantoate-beta-alanine ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0009058biological_processbiosynthetic process
B0015940biological_processpantothenate biosynthetic process
B0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ANP A 271
ChainResidue
APRO30
ALYS152
AASP153
APRO177
ATHR178
AGLN179
ALEU187
ASER188
ASER189
AARG190
AMG273
AMSE32
APRO274
ABAL275
AHOH287
AHOH294
AHOH306
AHIS36
AGLY38
AHIS39
ALEU42
ATYR73
ALEU149
AGLY150

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PRO A 274
ChainResidue
AMSE32
AGLN63
AMSE131
AVAL134
AVAL135
AGLN156
AANP271
AHOH307

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 273
ChainResidue
AMSE32
AGLY33
ATYR73
ASER189
AANP271

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PRO B 272
ChainResidue
BPRO30
BGLN63
BVAL134
BGLN156
BANP271
BHOH285

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BAL A 275
ChainResidue
AMSE32
AGLN63
AARG124
AHIS127
AASP153
AARG190
AANP271

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ANP B 271
ChainResidue
BPRO30
BTHR31
BMSE32
BHIS36
BGLY38
BHIS39
BLEU42
BTYR73
BLEU149
BGLY150
BLYS152
BASP153
BPRO177
BTHR178
BGLN179
BLEU187
BSER188
BSER189
BARG190
BPRO272
BBAL275
BHOH279
BHOH301
BHOH302

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BAL B 275
ChainResidue
BMSE32
BGLN63
BARG124
BASP153
BARG190
BANP271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00158
ChainResidueDetails
AHIS39
BHIS39

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00158
ChainResidueDetails
AMSE32
BLEU187
AGLN63
AGLY150
AGLN156
ALEU187
BMSE32
BGLN63
BGLY150
BGLN156

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PDB entries from 2024-07-24

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