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 | 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 | 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 | THR10 | |
A | GLU126 | |
A | SER151 | |
A | SER186 | |
A | HIS209 | |
A | GLY215 | |
A | SER222 | |
A | ASN227 | |
A | LYS228 | |
B | THR10 | |
B | GLY11 | |
A | GLY11 | |
B | SER12 | |
B | ILE13 | |
B | GLY36 | |
B | LYS37 | |
B | ASN38 | |
B | ASN124 | |
B | LYS125 | |
B | GLU126 | |
B | SER151 | |
B | SER186 | |
A | SER12 | |
B | HIS209 | |
B | GLY215 | |
B | SER222 | |
B | ASN227 | |
B | LYS228 | |
A | ILE13 | |
A | GLY36 | |
A | LYS37 | |
A | ASN38 | |
A | ASN124 | |
A | LYS125 |
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 |