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3ND7

Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0015937biological_processcoenzyme A biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0009058biological_processbiosynthetic process
B0015937biological_processcoenzyme A biosynthetic process
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0009058biological_processbiosynthetic process
C0015937biological_processcoenzyme A biosynthetic process
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0009058biological_processbiosynthetic process
D0015937biological_processcoenzyme A biosynthetic process
D0016740molecular_functiontransferase activity
D0016779molecular_functionnucleotidyltransferase activity
E0000166molecular_functionnucleotide binding
E0003824molecular_functioncatalytic activity
E0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0009058biological_processbiosynthetic process
E0015937biological_processcoenzyme A biosynthetic process
E0016740molecular_functiontransferase activity
E0016779molecular_functionnucleotidyltransferase activity
F0000166molecular_functionnucleotide binding
F0003824molecular_functioncatalytic activity
F0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0009058biological_processbiosynthetic process
F0015937biological_processcoenzyme A biosynthetic process
F0016740molecular_functiontransferase activity
F0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PNY A 501
ChainResidue
AGLY9
AHOH200
CGLU135
ASER10
AGLN73
ALEU74
ATHR75
ATYR99
AMET106
AASN107
AHOH193

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PNY B 502
ChainResidue
BPHE37
BGLN73
BLEU74
BTHR75
BTYR99
BILE103
BMET106
BASN107
BHOH172
BHOH173
FGLU135
FPHE139

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PNY C 503
ChainResidue
CGLN73
CLEU74
CTHR75
CARG89
CTYR99
CILE103
CMET106
CASN107
CHOH182
EGLU135

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PNY D 504
ChainResidue
BLEU132
BGLU135
DPRO8
DGLN73
DLEU74
DTHR75
DTYR99
DILE103
DMET106
DASN107
DHOH178
DHOH192
DHOH199

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PNY E 505
ChainResidue
AGLU135
EGLY9
EGLN73
ELEU74
ETHR75
EARG89
ETYR99
EMET106
EASN107
EHOH179
EHOH225

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PNY F 506
ChainResidue
DGLU135
FLEU74
FTHR75
FTYR99
FMET106
FASN107
FHOH172
FHOH182

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues60
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21912874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ND6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21912874","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3ND7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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