2LH5
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 | 4 |
Details | BINDING SITE FOR RESIDUE F A 154 |
Chain | Residue |
A | HIS63 |
A | VAL67 |
A | HEM155 |
A | HOH218 |
site_id | AC2 |
Number of Residues | 13 |
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 | F154 |
A | LEU43 |
A | PHE44 |
A | SER45 |
A | HIS63 |
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 |