3PNB
Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis in complex with coenzyme A
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 |
A | 0034214 | biological_process | protein hexamerization |
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 |
B | 0034214 | biological_process | protein hexamerization |
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 |
C | 0034214 | biological_process | protein hexamerization |
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 |
D | 0034214 | biological_process | protein hexamerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE COA A 162 |
Chain | Residue |
A | GLY8 |
A | SER128 |
A | GLU132 |
A | HOH158 |
A | HOH160 |
A | HOH167 |
A | HOH186 |
A | HOH203 |
A | HOH212 |
A | HOH272 |
A | SER9 |
A | GLY71 |
A | LEU72 |
A | VAL73 |
A | LYS87 |
A | ASP94 |
A | TYR97 |
A | ASN105 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE COA B 162 |
Chain | Residue |
B | GLY8 |
B | SER9 |
B | GLY71 |
B | LEU72 |
B | VAL73 |
B | LYS87 |
B | ASP94 |
B | TYR97 |
B | ASN105 |
B | SER128 |
B | GLU132 |
B | HOH167 |
B | HOH172 |
B | HOH190 |
B | HOH198 |
B | HOH264 |
B | HOH301 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE COA C 162 |
Chain | Residue |
C | GLY8 |
C | SER9 |
C | LEU36 |
C | GLY71 |
C | LEU72 |
C | VAL73 |
C | ASP94 |
C | TYR97 |
C | ASN105 |
C | SER128 |
C | GLU132 |
C | HOH166 |
C | HOH173 |
C | HOH181 |
C | HOH182 |
C | HOH189 |
C | HOH233 |
C | HOH265 |
C | HOH281 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE COA D 162 |
Chain | Residue |
D | GLY8 |
D | SER9 |
D | GLY71 |
D | LEU72 |
D | VAL73 |
D | LYS87 |
D | ASP94 |
D | TYR97 |
D | ASN105 |
D | SER128 |
D | GLU132 |
D | HOH169 |
D | HOH170 |
D | HOH178 |
D | HOH186 |
D | HOH230 |
D | HOH295 |
D | HOH555 |
D | HOH565 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:20851704, ECO:0007744|PDB:3NBK |
Chain | Residue | Details |
A | SER9 | |
A | VAL73 | |
B | SER9 | |
B | VAL73 | |
C | SER9 | |
C | VAL73 | |
D | SER9 | |
D | VAL73 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:23151631, ECO:0000305|PubMed:20851704, ECO:0007744|PDB:3NBA, ECO:0007744|PDB:3UC5 |
Chain | Residue | Details |
A | HIS17 | |
D | HIS17 | |
D | GLY88 | |
D | TYR122 | |
A | GLY88 | |
A | TYR122 | |
B | HIS17 | |
B | GLY88 | |
B | TYR122 | |
C | HIS17 | |
C | GLY88 | |
C | TYR122 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | LYS41 | |
A | LYS87 | |
B | LYS41 | |
B | LYS87 | |
C | LYS41 | |
C | LYS87 | |
D | LYS41 | |
D | LYS87 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:23151631, ECO:0007744|PDB:3UC5 |
Chain | Residue | Details |
A | GLU98 | |
B | GLU98 | |
C | GLU98 | |
D | GLU98 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20851704, ECO:0007744|PDB:3NBK |
Chain | Residue | Details |
A | ASN105 | |
B | ASN105 | |
C | ASN105 | |
D | ASN105 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23151631, ECO:0000305|PubMed:20851704, ECO:0007744|PDB:3NBA, ECO:0007744|PDB:3UC5 |
Chain | Residue | Details |
A | THR118 | |
B | THR118 | |
C | THR118 | |
D | THR118 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | HIS17 | |
B | HIS17 | |
C | HIS17 | |
D | HIS17 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 | |
C | THR2 | |
D | THR2 |