2GDS
Interrupting the Hydrogen Bonding Network at the Active Site of Human Manganese Superoxide Dismutase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004784 | molecular_function | superoxide dismutase activity |
| C | 0006801 | biological_process | superoxide metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004784 | molecular_function | superoxide dismutase activity |
| D | 0006801 | biological_process | superoxide metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 199 |
| Chain | Residue |
| A | HIS26 |
| A | HIS74 |
| A | ASP159 |
| A | HIS163 |
| A | HOH5011 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 200 |
| Chain | Residue |
| B | HOH945 |
| B | HOH5022 |
| B | HIS26 |
| B | HIS74 |
| B | ASP159 |
| B | HIS163 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 201 |
| Chain | Residue |
| C | HIS26 |
| C | HIS74 |
| C | ASP159 |
| C | HIS163 |
| C | HOH5033 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 202 |
| Chain | Residue |
| D | HIS26 |
| D | HIS74 |
| D | ASP159 |
| D | HIS163 |
| D | HOH5044 |
Functional Information from PROSITE/UniProt
| site_id | PS00088 |
| Number of Residues | 8 |
| Details | SOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY |
| Chain | Residue | Details |
| A | ASP159-TYR166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K |
| Chain | Residue | Details |
| A | HIS26 | |
| C | HIS74 | |
| C | ASP159 | |
| C | HIS163 | |
| D | HIS26 | |
| D | HIS74 | |
| D | ASP159 | |
| D | HIS163 | |
| A | HIS74 | |
| A | ASP159 | |
| A | HIS163 | |
| B | HIS26 | |
| B | HIS74 | |
| B | ASP159 | |
| B | HIS163 | |
| C | HIS26 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:10334867, ECO:0000269|PubMed:16399855 |
| Chain | Residue | Details |
| A | TYR34 | |
| B | TYR34 | |
| C | TYR34 | |
| D | TYR34 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671 |
| Chain | Residue | Details |
| A | LYS44 | |
| C | LYS51 | |
| C | LYS98 | |
| C | LYS106 | |
| D | LYS44 | |
| D | LYS51 | |
| D | LYS98 | |
| D | LYS106 | |
| A | LYS51 | |
| A | LYS98 | |
| A | LYS106 | |
| B | LYS44 | |
| B | LYS51 | |
| B | LYS98 | |
| B | LYS106 | |
| C | LYS44 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09671 |
| Chain | Residue | Details |
| A | LYS90 | |
| A | LYS178 | |
| B | LYS90 | |
| B | LYS178 | |
| C | LYS90 | |
| C | LYS178 | |
| D | LYS90 | |
| D | LYS178 |
