2EB8
Crystal Structure of Cu(II)(Sal-Phe)/apo-Myoglobin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005344 | molecular_function | oxygen carrier activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0015671 | biological_process | oxygen transport |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016528 | cellular_component | sarcoplasm |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0019825 | molecular_function | oxygen binding |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0098809 | molecular_function | nitrite reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
Chain | Residue |
A | ARG45 |
A | LYS63 |
A | HIS93 |
A | HIS116 |
A | PO42003 |
A | HOH2049 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 2002 |
Chain | Residue |
A | LYS16 |
A | HIS119 |
A | HOH2037 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 2003 |
Chain | Residue |
A | ARG45 |
A | LYS63 |
A | HIS64 |
A | THR67 |
A | LYS87 |
A | SER92 |
A | GLU148 |
A | PO42001 |
A | HOH2024 |
A | HOH2049 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 2004 |
Chain | Residue |
A | HIS113 |
A | SER117 |
A | HOH2076 |
A | HOH2124 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 2005 |
Chain | Residue |
A | HIS93 |
A | LYS147 |
A | HOH2067 |
A | HOH2129 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CUP A 1001 |
Chain | Residue |
A | PHE43 |
A | HIS64 |
A | VAL68 |
A | GLN91 |
A | SER92 |
A | THR95 |
A | ILE99 |
A | LEU104 |
A | HOH2135 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO |
Chain | Residue | Details |
A | HIS64 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959, ECO:0007744|PDB:4MBN, ECO:0007744|PDB:5MBN |
Chain | Residue | Details |
A | HIS93 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 |
Chain | Residue | Details |
A | SER3 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247 |
Chain | Residue | Details |
A | THR67 |