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5H7X

Crystal structure of the complex of Phosphopantetheine adenylyltransferase from Acinetobacter baumannii with 2-hydroxy-1,2,3-propane tricarboxylate at 1.76 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0015937biological_processcoenzyme A biosynthetic process
A0016779molecular_functionnucleotidyltransferase activity
B0003824molecular_functioncatalytic activity
B0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0009058biological_processbiosynthetic process
B0015937biological_processcoenzyme A biosynthetic process
B0016779molecular_functionnucleotidyltransferase activity
C0003824molecular_functioncatalytic activity
C0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0009058biological_processbiosynthetic process
C0015937biological_processcoenzyme A biosynthetic process
C0016779molecular_functionnucleotidyltransferase activity
D0003824molecular_functioncatalytic activity
D0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0009058biological_processbiosynthetic process
D0015937biological_processcoenzyme A biosynthetic process
D0016779molecular_functionnucleotidyltransferase activity
E0003824molecular_functioncatalytic activity
E0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0009058biological_processbiosynthetic process
E0015937biological_processcoenzyme A biosynthetic process
E0016779molecular_functionnucleotidyltransferase activity
F0003824molecular_functioncatalytic activity
F0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0009058biological_processbiosynthetic process
F0015937biological_processcoenzyme A biosynthetic process
F0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue CIT A 201
ChainResidue
AGLY10
AHOH334
AHOH382
ATHR11
APHE12
AHIS19
ASER129
ASER130
ATHR131
AHOH305
AHOH316

site_idAC2
Number of Residues10
Detailsbinding site for residue CIT B 201
ChainResidue
BGLY10
BTHR11
BPHE12
BHIS19
BSER129
BSER130
BTHR131
BHOH302
BHOH303
BHOH312

site_idAC3
Number of Residues13
Detailsbinding site for residue CIT C 201
ChainResidue
CGLY10
CTHR11
CPHE12
CHIS19
CSER129
CSER130
CTHR131
CHOH301
CHOH304
CHOH306
CHOH307
CHOH337
CHOH370

site_idAC4
Number of Residues11
Detailsbinding site for residue CIT D 201
ChainResidue
DGLY10
DTHR11
DPHE12
DHIS19
DSER129
DSER130
DTHR131
DHOH303
DHOH306
DHOH325
DHOH336

site_idAC5
Number of Residues12
Detailsbinding site for residue CIT E 201
ChainResidue
EGLY10
ETHR11
EPHE12
EHIS19
EARG92
ESER129
ESER130
ETHR131
EHOH301
EHOH325
EHOH338
EHOH384

site_idAC6
Number of Residues12
Detailsbinding site for residue CIT F 201
ChainResidue
FGLY10
FTHR11
FPHE12
FHIS19
FSER129
FSER130
FTHR131
FHOH301
FHOH303
FHOH308
FHOH310
FHOH343

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151
ChainResidueDetails
ATHR11
BHIS19
BLYS43
BLEU75
BARG89
BGLY90
BGLU100
BTYR125
CTHR11
CHIS19
CLYS43
AHIS19
CLEU75
CARG89
CGLY90
CGLU100
CTYR125
DTHR11
DHIS19
DLYS43
DLEU75
DARG89
ALYS43
DGLY90
DGLU100
DTYR125
ETHR11
EHIS19
ELYS43
ELEU75
EARG89
EGLY90
EGLU100
ALEU75
ETYR125
FTHR11
FHIS19
FLYS43
FLEU75
FARG89
FGLY90
FGLU100
FTYR125
AARG89
AGLY90
AGLU100
ATYR125
BTHR11

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
ChainResidueDetails
AHIS19
BHIS19
CHIS19
DHIS19
EHIS19
FHIS19

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PDB entries from 2024-09-11

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