4NAU
S. aureus CoaD with Inhibitor
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AGS A 201 |
Chain | Residue |
A | PRO9 |
A | SER121 |
A | TYR125 |
A | ILE128 |
A | SER129 |
A | SER130 |
A | SER131 |
A | HOH324 |
A | HOH327 |
A | SER11 |
A | PHE12 |
A | GLY18 |
A | HIS19 |
A | ILE22 |
A | ARG89 |
A | GLY90 |
A | ARG92 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2W3 A 202 |
Chain | Residue |
A | LEU38 |
A | SER41 |
A | LYS43 |
A | PHE71 |
A | GLY73 |
A | LEU74 |
A | LEU75 |
A | ARG89 |
A | TYR99 |
A | MET106 |
A | ASN107 |
A | HOH312 |
B | GLU135 |
B | TYR139 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AGS B 201 |
Chain | Residue |
A | ARG102 |
B | PRO9 |
B | SER11 |
B | PHE12 |
B | GLY18 |
B | HIS19 |
B | ARG89 |
B | GLY90 |
B | ARG92 |
B | SER121 |
B | TYR125 |
B | ILE128 |
B | SER129 |
B | SER130 |
B | SER131 |
B | HOH310 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AGS C 201 |
Chain | Residue |
C | SER11 |
C | PHE12 |
C | GLY18 |
C | HIS19 |
C | ARG89 |
C | GLY90 |
C | ARG92 |
C | SER121 |
C | TYR125 |
C | ILE128 |
C | SER129 |
C | SER130 |
C | SER131 |
C | HOH301 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | SER11 | |
C | LYS43 | |
C | LEU75 | |
C | ARG89 | |
A | LYS43 | |
A | LEU75 | |
A | ARG89 | |
B | SER11 | |
B | LYS43 | |
B | LEU75 | |
B | ARG89 | |
C | SER11 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU |
Chain | Residue | Details |
A | HIS19 | |
A | TYR125 | |
B | HIS19 | |
B | TYR125 | |
C | HIS19 | |
C | TYR125 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAT, ECO:0007744|PDB:4NAU |
Chain | Residue | Details |
A | GLY90 | |
B | GLY90 | |
C | GLY90 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH |
Chain | Residue | Details |
A | GLU100 | |
B | GLU100 | |
C | GLU100 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH, ECO:0007744|PDB:4NAU |
Chain | Residue | Details |
A | SER121 | |
B | SER121 | |
C | SER121 |