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6B7E

Crystal structure of E.coli Phosphopantetheine Adenylyltransferase (PPAT/CoaD) in complex with (R)-4-(5-(difluoromethyl)-1H-imidazol-1-yl)-3,3-dimethylisochroman-1-one

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0015937biological_processcoenzyme A biosynthetic process
A0016779molecular_functionnucleotidyltransferase activity
A0042802molecular_functionidentical protein binding
B0003824molecular_functioncatalytic activity
B0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0009058biological_processbiosynthetic process
B0015937biological_processcoenzyme A biosynthetic process
B0016779molecular_functionnucleotidyltransferase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 201
ChainResidue
ASER121
ALYS122
AHOH309
AHOH310
BHIS104
BARG107

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 202
ChainResidue
ASER129
AHOH317
AHOH382
AHIS18
AARG91
ASER128

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 203
ChainResidue
ALEU73
ALEU102
ALEU131
AHOH304
AHOH312

site_idAC4
Number of Residues5
Detailsbinding site for residue DMS A 204
ChainResidue
ATHR26
AGLN27
APHE29
AASP30
BLYS3

site_idAC5
Number of Residues15
Detailsbinding site for residue CWA B 201
ChainResidue
BPRO8
BGLY9
BALA37
BPHE70
BLEU73
BMET74
BARG88
BTYR98
BLEU102
BASN106
BLEU131
BGLU134
BHIS138
BSO4205
BHOH397

site_idAC6
Number of Residues7
Detailsbinding site for residue SO4 B 202
ChainResidue
AHIS104
AARG107
BSER121
BLYS122
BHOH307
BHOH311
BHOH334

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 B 203
ChainResidue
BSER39
BPRO40
BSER41
BGLU134
BHIS138
BHOH351

site_idAC8
Number of Residues7
Detailsbinding site for residue SO4 B 204
ChainResidue
BHIS18
BARG91
BSER128
BSER129
BHOH301
BHOH313
BHOH333

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 B 205
ChainResidue
BGLY9
BTHR10
BLYS42
BARG88
BCWA201
BHOH301

site_idAD1
Number of Residues7
Detailsbinding site for residue DMS B 206
ChainResidue
AGLN2
ALYS3
BTHR26
BGLN27
BMET28
BPHE29
BASP30

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8
ChainResidueDetails
ATYR7
BTRP124
AHIS18
AGLY89
AGLU99
ATRP124
BTYR7
BHIS18
BGLY89
BGLU99

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11812124, ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T, ECO:0007744|PDB:1QJC
ChainResidueDetails
ATHR10
ALYS42
AMET74
BTHR10
BLYS42
BMET74

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1QJC
ChainResidueDetails
AARG88
BARG88

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:11812124
ChainResidueDetails
AHIS18
BHIS18

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 299
ChainResidueDetails
AHIS18electrostatic stabiliser, hydrogen bond donor
ALYS42attractive charge-charge interaction, electrostatic stabiliser
AARG91attractive charge-charge interaction, electrostatic stabiliser
ASER129electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 299
ChainResidueDetails
BHIS18electrostatic stabiliser, hydrogen bond donor
BLYS42attractive charge-charge interaction, electrostatic stabiliser
BARG91attractive charge-charge interaction, electrostatic stabiliser
BSER129electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-06-26

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