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
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0009058 | biological_process | biosynthetic process |
A | 0015937 | biological_process | coenzyme A biosynthetic process |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0009058 | biological_process | biosynthetic process |
B | 0015937 | biological_process | coenzyme A biosynthetic process |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0009058 | biological_process | biosynthetic process |
C | 0015937 | biological_process | coenzyme A biosynthetic process |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0009058 | biological_process | biosynthetic process |
D | 0015937 | biological_process | coenzyme A biosynthetic process |
D | 0016779 | molecular_function | nucleotidyltransferase activity |
E | 0003824 | molecular_function | catalytic activity |
E | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0009058 | biological_process | biosynthetic process |
E | 0015937 | biological_process | coenzyme A biosynthetic process |
E | 0016779 | molecular_function | nucleotidyltransferase activity |
F | 0003824 | molecular_function | catalytic activity |
F | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0009058 | biological_process | biosynthetic process |
F | 0015937 | biological_process | coenzyme A biosynthetic process |
F | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PNY A 501 |
Chain | Residue |
A | GLY9 |
A | HOH200 |
C | GLU135 |
A | SER10 |
A | GLN73 |
A | LEU74 |
A | THR75 |
A | TYR99 |
A | MET106 |
A | ASN107 |
A | HOH193 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PNY B 502 |
Chain | Residue |
B | PHE37 |
B | GLN73 |
B | LEU74 |
B | THR75 |
B | TYR99 |
B | ILE103 |
B | MET106 |
B | ASN107 |
B | HOH172 |
B | HOH173 |
F | GLU135 |
F | PHE139 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PNY C 503 |
Chain | Residue |
C | GLN73 |
C | LEU74 |
C | THR75 |
C | ARG89 |
C | TYR99 |
C | ILE103 |
C | MET106 |
C | ASN107 |
C | HOH182 |
E | GLU135 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PNY D 504 |
Chain | Residue |
B | LEU132 |
B | GLU135 |
D | PRO8 |
D | GLN73 |
D | LEU74 |
D | THR75 |
D | TYR99 |
D | ILE103 |
D | MET106 |
D | ASN107 |
D | HOH178 |
D | HOH192 |
D | HOH199 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PNY E 505 |
Chain | Residue |
A | GLU135 |
E | GLY9 |
E | GLN73 |
E | LEU74 |
E | THR75 |
E | ARG89 |
E | TYR99 |
E | MET106 |
E | ASN107 |
E | HOH179 |
E | HOH225 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PNY F 506 |
Chain | Residue |
D | GLU135 |
F | LEU74 |
F | THR75 |
F | TYR99 |
F | MET106 |
F | ASN107 |
F | HOH172 |
F | HOH182 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | SER10 | |
D | SER10 | |
D | LYS42 | |
D | ARG89 | |
E | SER10 | |
E | LYS42 | |
E | ARG89 | |
F | SER10 | |
F | LYS42 | |
F | ARG89 | |
A | LYS42 | |
A | ARG89 | |
B | SER10 | |
B | LYS42 | |
B | ARG89 | |
C | SER10 | |
C | LYS42 | |
C | ARG89 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6 |
Chain | Residue | Details |
A | HIS18 | |
C | GLY90 | |
C | GLU100 | |
C | TYR125 | |
D | HIS18 | |
D | GLY90 | |
D | GLU100 | |
D | TYR125 | |
E | HIS18 | |
E | GLY90 | |
E | GLU100 | |
A | GLY90 | |
E | TYR125 | |
F | HIS18 | |
F | GLY90 | |
F | GLU100 | |
F | TYR125 | |
A | GLU100 | |
A | TYR125 | |
B | HIS18 | |
B | GLY90 | |
B | GLU100 | |
B | TYR125 | |
C | HIS18 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7 |
Chain | Residue | Details |
A | THR75 | |
B | THR75 | |
C | THR75 | |
D | THR75 | |
E | THR75 | |
F | THR75 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | HIS18 | |
B | HIS18 | |
C | HIS18 | |
D | HIS18 | |
E | HIS18 | |
F | HIS18 |