3R0I
IspC in complex with an N-methyl-substituted hydroxamic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| A | 0070402 | molecular_function | NADPH binding |
| A | 1990065 | cellular_component | Dxr protein complex |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| B | 0070402 | molecular_function | NADPH binding |
| B | 1990065 | cellular_component | Dxr protein complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 990 |
| Chain | Residue |
| A | ASP150 |
| A | GLU152 |
| A | GLU231 |
| A | HOH432 |
| A | C0K991 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 990 |
| Chain | Residue |
| B | C0K991 |
| B | ASP150 |
| B | GLU152 |
| B | GLU231 |
| B | HOH580 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE C0K A 991 |
| Chain | Residue |
| A | ASP150 |
| A | SER151 |
| A | GLU152 |
| A | GLY185 |
| A | SER186 |
| A | SER222 |
| A | ASN227 |
| A | LYS228 |
| A | GLU231 |
| A | SER254 |
| A | MET276 |
| A | HOH405 |
| A | HOH432 |
| A | HOH476 |
| A | HOH548 |
| A | HOH689 |
| A | MN990 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE C0K B 991 |
| Chain | Residue |
| B | ASP150 |
| B | SER151 |
| B | GLU152 |
| B | GLY185 |
| B | SER186 |
| B | SER222 |
| B | ASN227 |
| B | LYS228 |
| B | GLU231 |
| B | SER254 |
| B | HOH399 |
| B | HOH414 |
| B | HOH456 |
| B | HOH580 |
| B | HOH629 |
| B | HOH727 |
| B | MN990 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15567415, ECO:0007744|PDB:1Q0Q |
| Chain | Residue | Details |
| A | SER12 | |
| A | ILE13 | |
| A | GLY36 | |
| A | LYS37 | |
| A | ASN38 | |
| A | ASN124 | |
| A | LYS125 | |
| A | GLU126 | |
| A | SER151 | |
| A | SER186 | |
| A | HIS209 | |
| A | GLY215 | |
| A | SER222 | |
| A | ASN227 | |
| A | LYS228 | |
| B | THR10 | |
| B | GLY11 | |
| B | SER12 | |
| B | ILE13 | |
| B | GLY36 | |
| B | LYS37 | |
| B | ASN38 | |
| B | ASN124 | |
| B | LYS125 | |
| B | GLU126 | |
| B | SER151 | |
| B | SER186 | |
| B | HIS209 | |
| B | GLY215 | |
| B | SER222 | |
| B | ASN227 | |
| B | LYS228 | |
| A | THR10 | |
| A | GLY11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12621040, ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP |
| Chain | Residue | Details |
| A | ASP150 | |
| A | GLU152 | |
| A | GLU231 | |
| B | ASP150 | |
| B | GLU152 | |
| B | GLU231 |
