6TH2
Crystal structure of Mycobacterium smegmatis CoaB in complex with CTP
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue CTP A 501 |
| Chain | Residue |
| A | MET275 |
| A | PHE332 |
| A | LYS350 |
| A | LYS354 |
| A | CA502 |
| A | HOH606 |
| A | HOH613 |
| A | HOH621 |
| A | HOH643 |
| A | HOH647 |
| A | HOH660 |
| A | ALA277 |
| A | HOH697 |
| B | LYS293 |
| B | LYS294 |
| B | HOH612 |
| A | VAL279 |
| A | ASP281 |
| A | ASP308 |
| A | ASP309 |
| A | VAL310 |
| A | LEU311 |
| A | GLY331 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | ASP281 |
| A | CTP501 |
| A | HOH621 |
| B | HOH612 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue ACT A 503 |
| Chain | Residue |
| A | ILE209 |
| A | GLY210 |
| A | ASN211 |
| A | ALA280 |
| A | HOH608 |
| A | HOH620 |
| A | HOH625 |
| B | ARG207 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue MES A 504 |
| Chain | Residue |
| A | SER213 |
| A | SER214 |
| A | GLY215 |
| A | LYS216 |
| A | GLN217 |
| A | GLY218 |
| A | ALA276 |
| A | ALA334 |
| A | HOH609 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue CTP B 501 |
| Chain | Residue |
| A | HOH601 |
| B | MET275 |
| B | ALA277 |
| B | VAL279 |
| B | ASP281 |
| B | ASP308 |
| B | ASP309 |
| B | VAL310 |
| B | LEU311 |
| B | GLY331 |
| B | PHE332 |
| B | LYS350 |
| B | LYS354 |
| B | CA502 |
| B | HOH627 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | ASP281 |
| B | CTP501 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue ACT B 503 |
| Chain | Residue |
| A | ARG207 |
| B | ILE209 |
| B | GLY210 |
| B | ASN211 |
| B | ALA280 |
| B | HOH608 |
| B | HOH610 |
| B | HOH668 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue MES B 504 |
| Chain | Residue |
| B | SER213 |
| B | SER214 |
| B | GLY215 |
| B | LYS216 |
| B | GLN217 |
| B | GLY218 |
| B | ALA276 |
| B | PHE332 |
| B | ALA334 |
| B | HOH605 |
| B | HOH721 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | binding site for residue CTP C 501 |
| Chain | Residue |
| D | HOH634 |
| D | HOH639 |
| C | MET275 |
| C | ALA277 |
| C | VAL279 |
| C | ASP281 |
| C | ASP308 |
| C | ASP309 |
| C | VAL310 |
| C | LEU311 |
| C | GLY331 |
| C | PHE332 |
| C | LYS350 |
| C | LYS354 |
| C | CA502 |
| C | HOH603 |
| C | HOH616 |
| C | HOH657 |
| C | HOH712 |
| D | LYS293 |
| D | LYS294 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 502 |
| Chain | Residue |
| C | ASP281 |
| C | CTP501 |
| C | HOH616 |
| D | HOH639 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue ACT C 503 |
| Chain | Residue |
| C | ILE209 |
| C | GLY210 |
| C | ASN211 |
| C | ALA280 |
| C | HOH605 |
| C | HOH607 |
| C | HOH632 |
| D | ARG207 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue ACT C 504 |
| Chain | Residue |
| C | ARG353 |
| C | HOH613 |
| C | HOH639 |
| D | ARG223 |
| D | LEU242 |
| D | ILE243 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue MES C 505 |
| Chain | Residue |
| C | SER213 |
| C | SER214 |
| C | GLY215 |
| C | LYS216 |
| C | GLN217 |
| C | GLY218 |
| C | ALA276 |
| C | ALA333 |
| C | ALA334 |
| C | HOH602 |
| site_id | AD5 |
| Number of Residues | 13 |
| Details | binding site for residue CTP D 501 |
| Chain | Residue |
| D | MET275 |
| D | ALA277 |
| D | VAL279 |
| D | ASP281 |
| D | ASP308 |
| D | ASP309 |
| D | VAL310 |
| D | LEU311 |
| D | PHE332 |
| D | LYS350 |
| D | ARG353 |
| D | LYS354 |
| D | CA502 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue CA D 502 |
| Chain | Residue |
| D | ASP281 |
| D | CTP501 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue ACT D 503 |
| Chain | Residue |
| C | ARG207 |
| D | ILE209 |
| D | GLY210 |
| D | ASN211 |
| D | ALA280 |
| D | HOH601 |
| D | HOH612 |
| D | HOH623 |
| site_id | AD8 |
| Number of Residues | 11 |
| Details | binding site for residue MES D 504 |
| Chain | Residue |
| D | SER213 |
| D | SER214 |
| D | GLY215 |
| D | GLN217 |
| D | GLY218 |
| D | ALA276 |
| D | PHE332 |
| D | VAL364 |
| D | HOH631 |
| D | HOH637 |
| D | HOH686 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6THC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02225","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TH2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02225","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6THC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02225","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6THC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6THC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
