2GNW
Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40W
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 | 15 |
Details | BINDING SITE FOR RESIDUE HEM A 166 |
Chain | Residue |
A | MET53 |
A | TYR111 |
A | VAL113 |
A | HIS117 |
A | PHE118 |
A | VAL121 |
A | VAL154 |
A | PHE54 |
A | LYS69 |
A | HIS73 |
A | SER76 |
A | VAL77 |
A | ARG103 |
A | LEU104 |
A | HIS108 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEM B 166 |
Chain | Residue |
B | MET53 |
B | LYS69 |
B | HIS73 |
B | VAL77 |
B | ARG103 |
B | LEU104 |
B | THR107 |
B | HIS108 |
B | TYR111 |
B | VAL113 |
B | HIS117 |
B | PHE118 |
B | VAL121 |
B | LEU153 |
B | VAL154 |
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 | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P68168 |
Chain | Residue | Details |
A | SER55 | |
B | SER55 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV |
Chain | Residue | Details |
A | LYS69 | |
B | LYS69 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV, ECO:0007744|PDB:2GNW |
Chain | Residue | Details |
A | HIS73 | |
B | HIS73 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV, ECO:0007744|PDB:2GNW |
Chain | Residue | Details |
A | ARG103 | |
A | THR107 | |
B | ARG103 | |
B | THR107 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV, ECO:0007744|PDB:2GNW |
Chain | Residue | Details |
A | HIS108 | |
B | HIS108 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Homodimerization => ECO:0000269|PubMed:10986467, ECO:0007744|PDB:1D8U |
Chain | Residue | Details |
A | LYS143 | |
B | LYS143 |