1VCG
Crystal Structure of IPP isomerase at P43212
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008299 | biological_process | isoprenoid biosynthetic process |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008299 | biological_process | isoprenoid biosynthetic process |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN A 501 |
| Chain | Residue |
| A | ALA65 |
| A | GLY190 |
| A | THR217 |
| A | TRP219 |
| A | GLY263 |
| A | GLY264 |
| A | TYR266 |
| A | ALA285 |
| A | ARG286 |
| A | MSE66 |
| A | THR67 |
| A | GLY94 |
| A | SER95 |
| A | ASN123 |
| A | HIS152 |
| A | LYS187 |
| A | VAL189 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN B 502 |
| Chain | Residue |
| B | ALA65 |
| B | MSE66 |
| B | THR67 |
| B | GLY94 |
| B | SER95 |
| B | ASN123 |
| B | HIS152 |
| B | LYS187 |
| B | VAL189 |
| B | GLY190 |
| B | THR217 |
| B | TRP219 |
| B | GLY263 |
| B | GLY264 |
| B | TYR266 |
| B | ALA285 |
| B | ARG286 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN C 503 |
| Chain | Residue |
| C | ALA65 |
| C | MSE66 |
| C | THR67 |
| C | GLY94 |
| C | SER95 |
| C | ASN123 |
| C | HIS152 |
| C | LYS187 |
| C | VAL189 |
| C | GLY190 |
| C | THR217 |
| C | TRP219 |
| C | GLY263 |
| C | GLY264 |
| C | TYR266 |
| C | ALA285 |
| C | ARG286 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN D 504 |
| Chain | Residue |
| D | ALA65 |
| D | MSE66 |
| D | THR67 |
| D | SER95 |
| D | ASN123 |
| D | HIS152 |
| D | LYS187 |
| D | VAL189 |
| D | GLY190 |
| D | THR217 |
| D | TRP219 |
| D | GLY263 |
| D | GLY264 |
| D | TYR266 |
| D | ALA285 |
| D | ARG286 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00354","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00354","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Crystal Structure of IPP isomerase at I422.","authors":["Wada T.","Park S.-Y.","Tame R.H.","Kuramitsu S.","Yokoyama S."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Crystal Structure of IPP isomerase at P43212.","authors":["Wada T.","Park S.-Y.","Tame R.H.","Kuramitsu S.","Yokoyama S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Crystal Structure of IPP isomerase at I422.","authors":["Wada T.","Park S.-Y.","Tame R.H.","Kuramitsu S.","Yokoyama S."]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Crystal Structure of IPP isomerase at P43212.","authors":["Wada T.","Park S.-Y.","Tame R.H.","Kuramitsu S.","Yokoyama S."]}}]} |
| Chain | Residue | Details |
