2GNV
Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40L
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0010167 | biological_process | response to nitrate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071731 | biological_process | response to nitric oxide |
| A | 0080033 | biological_process | response to nitrite |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0010167 | biological_process | response to nitrate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071731 | biological_process | response to nitric oxide |
| B | 0080033 | biological_process | response to nitrite |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM A 166 |
| Chain | Residue |
| A | ALA50 |
| A | VAL121 |
| A | TYR150 |
| A | HOH393 |
| A | PHE54 |
| A | HIS73 |
| A | ARG103 |
| A | LEU104 |
| A | THR107 |
| A | HIS108 |
| A | TYR111 |
| A | HIS117 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM B 166 |
| Chain | Residue |
| B | ALA50 |
| B | LYS69 |
| B | HIS73 |
| B | MET80 |
| B | ARG103 |
| B | LEU104 |
| B | THR107 |
| B | HIS108 |
| B | TYR111 |
| B | HIS117 |
| B | PHE118 |
| B | VAL121 |
| B | TYR150 |
| B | LEU153 |
| B | HOH361 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DIO B 301 |
| Chain | Residue |
| B | LEU40 |
| B | ILE43 |
| B | LEU70 |
| B | HIS73 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DIO A 302 |
| Chain | Residue |
| A | PHE39 |
| A | LEU40 |
| A | HIS73 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DIO B 303 |
| Chain | Residue |
| B | TRP25 |
| B | SER32 |
| B | ILE35 |
| B | ALA36 |
| B | PHE78 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DIO A 304 |
| Chain | Residue |
| A | TRP25 |
| A | SER32 |
| A | ILE35 |
| A | ALA36 |
| A | ALA74 |
| A | PHE78 |
| A | HOH319 |
Functional Information from PROSITE/UniProt
| site_id | PS00208 |
| Number of Residues | 12 |
| Details | PLANT_GLOBIN Plant hemoglobins signature. NPkLktHAmsvF |
| Chain | Residue | Details |
| A | ASN67-PHE78 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 300 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Homodimerization","evidences":[{"source":"PubMed","id":"10986467","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893175","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P68168","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10986467","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893175","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"distal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10986467","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893175","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10986467","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893175","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10986467","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893175","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GNW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Homodimerization","evidences":[{"source":"PubMed","id":"10986467","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D8U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
