6TGV
Crystal structure of Mycobacterium smegmatis CoaBC in complex with CTP and FMN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004632 | molecular_function | phosphopantothenate--cysteine ligase activity |
| A | 0004633 | molecular_function | phosphopantothenoylcysteine decarboxylase activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0015941 | biological_process | pantothenate catabolic process |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071513 | cellular_component | phosphopantothenoylcysteine decarboxylase complex |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004632 | molecular_function | phosphopantothenate--cysteine ligase activity |
| B | 0004633 | molecular_function | phosphopantothenoylcysteine decarboxylase activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0015941 | biological_process | pantothenate catabolic process |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071513 | cellular_component | phosphopantothenoylcysteine decarboxylase complex |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004632 | molecular_function | phosphopantothenate--cysteine ligase activity |
| C | 0004633 | molecular_function | phosphopantothenoylcysteine decarboxylase activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0015941 | biological_process | pantothenate catabolic process |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0016874 | molecular_function | ligase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071513 | cellular_component | phosphopantothenoylcysteine decarboxylase complex |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004632 | molecular_function | phosphopantothenate--cysteine ligase activity |
| D | 0004633 | molecular_function | phosphopantothenoylcysteine decarboxylase activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0015937 | biological_process | coenzyme A biosynthetic process |
| D | 0015941 | biological_process | pantothenate catabolic process |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0016874 | molecular_function | ligase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071513 | cellular_component | phosphopantothenoylcysteine decarboxylase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue CTP A 501 |
| Chain | Residue |
| A | MET275 |
| A | ALA334 |
| A | LYS350 |
| A | MG505 |
| A | ALA277 |
| A | VAL279 |
| A | ASP281 |
| A | ASP309 |
| A | VAL310 |
| A | LEU311 |
| A | PHE332 |
| A | ALA333 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | LEU43 |
| A | GLY47 |
| A | ALA48 |
| A | HOH602 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | LYS19 |
| A | LEU163 |
| A | FMN506 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLY142 |
| A | VAL144 |
| A | ALA180 |
| A | ASP181 |
| A | ALA182 |
| A | LEU183 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 505 |
| Chain | Residue |
| A | ASP281 |
| A | CTP501 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue FMN A 506 |
| Chain | Residue |
| A | ALA12 |
| A | GLY13 |
| A | ILE15 |
| A | THR39 |
| A | SER41 |
| A | PHE45 |
| A | VAL63 |
| A | PHE64 |
| A | HIS72 |
| A | THR88 |
| A | ALA89 |
| A | ASP90 |
| A | LEU91 |
| A | ALA100 |
| A | ASP101 |
| A | ALA120 |
| A | MET121 |
| A | EDO503 |
| B | ALA53 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue CTP B 501 |
| Chain | Residue |
| B | MET275 |
| B | ALA277 |
| B | VAL279 |
| B | ALA280 |
| B | ASP308 |
| B | ASP309 |
| B | VAL310 |
| B | LEU311 |
| B | PHE332 |
| B | ALA333 |
| B | ALA334 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | ARG6 |
| B | ILE7 |
| B | SER33 |
| B | ARG35 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | ALA16 |
| B | LYS19 |
| B | ARG162 |
| B | LEU163 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue FMN B 504 |
| Chain | Residue |
| B | ALA12 |
| B | GLY13 |
| B | GLY14 |
| B | ILE15 |
| B | THR39 |
| B | SER41 |
| B | PHE45 |
| B | THR88 |
| B | ALA89 |
| B | LEU91 |
| B | ALA120 |
| B | MET121 |
| B | HOH602 |
| D | VAL63 |
| D | PHE64 |
| D | ALA100 |
| D | ASP101 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue CTP C 501 |
| Chain | Residue |
| C | MET275 |
| C | ALA277 |
| C | VAL279 |
| C | ALA280 |
| C | ASP308 |
| C | ASP309 |
| C | VAL310 |
| C | LEU311 |
| C | PHE332 |
| C | ALA334 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 502 |
| Chain | Residue |
| C | VAL144 |
| C | ALA180 |
| C | ASP181 |
| C | ALA182 |
| C | LEU183 |
| C | PRO184 |
| site_id | AD4 |
| Number of Residues | 20 |
| Details | binding site for residue FMN C 503 |
| Chain | Residue |
| B | PHE64 |
| B | VAL67 |
| B | HIS72 |
| B | ALA100 |
| C | ALA12 |
| C | GLY13 |
| C | GLY14 |
| C | ILE15 |
| C | THR39 |
| C | SER41 |
| C | PHE45 |
| C | THR88 |
| C | ALA89 |
| C | ASP90 |
| C | LEU91 |
| C | ALA120 |
| C | MET121 |
| C | HOH601 |
| C | HOH604 |
| B | VAL63 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue CTP D 501 |
| Chain | Residue |
| D | MET275 |
| D | ALA277 |
| D | VAL279 |
| D | ASP281 |
| D | ASP308 |
| D | VAL310 |
| D | LEU311 |
| D | GLY331 |
| D | PHE332 |
| D | ALA333 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| D | GLU147 |
| D | ALA226 |
| D | GLY229 |
| D | ALA230 |
| site_id | AD7 |
| Number of Residues | 18 |
| Details | binding site for residue FMN D 503 |
| Chain | Residue |
| C | VAL63 |
| C | PHE64 |
| C | HIS72 |
| C | ALA100 |
| D | ALA12 |
| D | GLY13 |
| D | GLY14 |
| D | ILE15 |
| D | THR39 |
| D | SER41 |
| D | PHE45 |
| D | THR88 |
| D | ALA89 |
| D | ASP90 |
| D | ARG94 |
| D | ALA120 |
| D | MET121 |
| D | HOH602 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33420031, ECO:0000269|Ref.4, ECO:0007744|PDB:4QJI, ECO:0007744|PDB:6TH2, ECO:0007744|PDB:6THC |
| Chain | Residue | Details |
| A | MET275 | |
| A | ASP308 | |
| B | MET275 | |
| B | ASP308 | |
| C | MET275 | |
| C | ASP308 | |
| D | MET275 | |
| D | ASP308 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:33420031, ECO:0000269|Ref.4, ECO:0007744|PDB:4QJI, ECO:0007744|PDB:6TH2 |
| Chain | Residue | Details |
| A | ASP281 | |
| B | ASP281 | |
| C | ASP281 | |
| D | ASP281 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:33420031, ECO:0000269|Ref.4, ECO:0007744|PDB:4QJI, ECO:0007744|PDB:6THC |
| Chain | Residue | Details |
| A | LYS291 | |
| B | LYS291 | |
| C | LYS291 | |
| D | LYS291 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33420031, ECO:0007744|PDB:6TH2, ECO:0007744|PDB:6THC |
| Chain | Residue | Details |
| A | LYS293 | |
| B | LYS293 | |
| C | LYS293 | |
| D | LYS293 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:33420031, ECO:0000269|Ref.4, ECO:0007744|PDB:4QJI, ECO:0007744|PDB:6TH2, ECO:0007744|PDB:6THC |
| Chain | Residue | Details |
| A | PHE332 | |
| D | PHE332 | |
| D | LYS350 | |
| D | LYS354 | |
| A | LYS350 | |
| A | LYS354 | |
| B | PHE332 | |
| B | LYS350 | |
| B | LYS354 | |
| C | PHE332 | |
| C | LYS350 | |
| C | LYS354 |
