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6B7A

Crystal structure of E.coli Phosphopantetheine Adenylyltransferase (PPAT/CoaD) in complex with 2-methyl-1H-benzo[d]imidazol-4-ol

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 CWM A 201
ChainResidue
ALEU73
AMET74
AALA75
AASN106
AGLU134
AVAL135

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 202
ChainResidue
AHOH336
AHOH341
BHIS104
BARG107
ASER121
ALYS122
AHOH310

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 203
ChainResidue
AHIS18
AARG91
ASER128
ASER129
AHOH302
AHOH303
AHOH323

site_idAC4
Number of Residues2
Detailsbinding site for residue PEG A 204
ChainResidue
AARG4
AHIS82

site_idAC5
Number of Residues4
Detailsbinding site for residue PEG A 205
ChainResidue
ATYR7
AARG88
AGLY89
AHOH333

site_idAC6
Number of Residues3
Detailsbinding site for residue CL A 206
ChainResidue
ASER41
AHIS138
AHOH402

site_idAC7
Number of Residues8
Detailsbinding site for residue CWM B 201
ChainResidue
BLEU73
BMET74
BALA75
BLEU102
BASN106
BGLU134
BVAL135
BHIS138

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 B 202
ChainResidue
BSER39
BPRO40
BSER41
BARG137
BHIS138
BHOH361

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 B 203
ChainResidue
AGLN2
BGLN27
BMET28
BPHE29
BASP30

site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 B 204
ChainResidue
AHIS104
AARG107
BSER121
BLYS122
BHOH336
BHOH373

site_idAD2
Number of Residues6
Detailsbinding site for residue PEG B 205
ChainResidue
BTYR7
BPRO8
BGLY9
BARG88
BGLY89
BPOP206

site_idAD3
Number of Residues11
Detailsbinding site for residue POP B 206
ChainResidue
BTHR10
BPHE11
BHIS18
BARG91
BSER129
BPEG205
BHOH302
BHOH303
BHOH313
BHOH316
BHOH328

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 2024-07-17

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