2LH3
X-RAY STRUCTURAL INVESTIGATION OF LEGHEMOGLOBIN. VI. STRUCTURE OF ACETATE-FERRILEGHEMOGLOBIN AT A RESOLUTION OF 2.0 ANGSTROMS (RUSSIAN)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009399 | biological_process | nitrogen fixation |
| A | 0009877 | biological_process | nodulation |
| A | 0010167 | biological_process | response to nitrate |
| A | 0015671 | biological_process | oxygen transport |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CYN A 154 |
| Chain | Residue |
| A | HIS63 |
| A | VAL67 |
| A | HEM155 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 155 |
| Chain | Residue |
| A | HIS97 |
| A | LYS100 |
| A | VAL102 |
| A | HIS106 |
| A | PHE107 |
| A | VAL110 |
| A | TYR138 |
| A | CYN154 |
| A | LEU43 |
| A | PHE44 |
| A | SER45 |
| A | HIS63 |
| A | VAL67 |
| A | LEU93 |
Functional Information from PROSITE/UniProt
| site_id | PS00208 |
| Number of Residues | 12 |
| Details | PLANT_GLOBIN Plant hemoglobins signature. NPeLqaHAgkvF |
| Chain | Residue | Details |
| A | ASN57-PHE68 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7643380, ECO:0000269|PubMed:8950274, ECO:0000269|Ref.5, ECO:0007744|PDB:1GDI, ECO:0007744|PDB:1GDJ, ECO:0007744|PDB:1GDK, ECO:0007744|PDB:1GDL, ECO:0007744|PDB:1LH1, ECO:0007744|PDB:1LH2, ECO:0007744|PDB:1LH3, ECO:0007744|PDB:1LH5, ECO:0007744|PDB:1LH6, ECO:0007744|PDB:1LH7, ECO:0007744|PDB:2GDM, ECO:0007744|PDB:2LH1, ECO:0007744|PDB:2LH2, ECO:0007744|PDB:2LH3, ECO:0007744|PDB:2LH5, ECO:0007744|PDB:2LH6, ECO:0007744|PDB:2LH7 |
| Chain | Residue | Details |
| A | PHE46 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7643380, ECO:0000269|Ref.5, ECO:0007744|PDB:2GDM, ECO:0007744|PDB:2LH2 |
| Chain | Residue | Details |
| A | ALA64 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7643380, ECO:0000269|PubMed:8950274, ECO:0000269|Ref.5, ECO:0007744|PDB:1GDI, ECO:0007744|PDB:1LH1, ECO:0007744|PDB:1LH2, ECO:0007744|PDB:1LH3, ECO:0007744|PDB:1LH5, ECO:0007744|PDB:1LH6, ECO:0007744|PDB:1LH7, ECO:0007744|PDB:2GDM, ECO:0007744|PDB:2LH1, ECO:0007744|PDB:2LH2, ECO:0007744|PDB:2LH3, ECO:0007744|PDB:2LH5, ECO:0007744|PDB:2LH6, ECO:0007744|PDB:2LH7 |
| Chain | Residue | Details |
| A | VAL67 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7643380, ECO:0000269|PubMed:8950274, ECO:0000269|Ref.5, ECO:0007744|PDB:1GDI, ECO:0007744|PDB:1GDJ, ECO:0007744|PDB:1GDK, ECO:0007744|PDB:1GDL, ECO:0007744|PDB:1LH1, ECO:0007744|PDB:1LH2, ECO:0007744|PDB:1LH3, ECO:0007744|PDB:1LH5, ECO:0007744|PDB:1LH6, ECO:0007744|PDB:1LH7, ECO:0007744|PDB:2GDM, ECO:0007744|PDB:2LH1, ECO:0007744|PDB:2LH2, ECO:0007744|PDB:2LH3, ECO:0007744|PDB:2LH5, ECO:0007744|PDB:2LH6, ECO:0007744|PDB:2LH7 |
| Chain | Residue | Details |
| A | VAL98 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|Ref.5, ECO:0007744|PDB:1LH3, ECO:0007744|PDB:1LH6, ECO:0007744|PDB:1LH7, ECO:0007744|PDB:2LH3, ECO:0007744|PDB:2LH6, ECO:0007744|PDB:2LH7 |
| Chain | Residue | Details |
| A | GLY101 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3C1F7 |
| Chain | Residue | Details |
| A | PHE46 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Nitrated tyrosine => ECO:0000250|UniProtKB:P02234 |
| Chain | Residue | Details |
| A | ASP139 |
