2HMQ
THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION
Replaces: 1HMQReplaces: 1HMMReplaces: 1HMNFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0015671 | biological_process | oxygen transport |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0015671 | biological_process | oxygen transport |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005344 | molecular_function | oxygen carrier activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0015671 | biological_process | oxygen transport |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005344 | molecular_function | oxygen carrier activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0015671 | biological_process | oxygen transport |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 114 |
| Chain | Residue |
| A | GLN60 |
| A | ALA64 |
| A | HOH146 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO A 115 |
| Chain | Residue |
| A | ASP106 |
| A | HOH135 |
| A | HIS25 |
| A | HIS54 |
| A | GLU58 |
| A | HIS73 |
| A | HIS77 |
| A | HIS101 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 114 |
| Chain | Residue |
| B | GLN60 |
| B | ALA64 |
| B | HOH185 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FEO B 115 |
| Chain | Residue |
| B | HIS25 |
| B | HIS54 |
| B | GLU58 |
| B | HIS73 |
| B | HIS77 |
| B | HIS101 |
| B | ASP106 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT C 114 |
| Chain | Residue |
| C | GLN60 |
| C | ALA64 |
| C | HOH211 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO C 115 |
| Chain | Residue |
| C | HIS25 |
| C | HIS54 |
| C | GLU58 |
| C | HIS73 |
| C | HIS77 |
| C | HIS101 |
| C | ASP106 |
| C | HOH147 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 114 |
| Chain | Residue |
| D | GLN60 |
| D | ALA64 |
| D | HOH293 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FEO D 115 |
| Chain | Residue |
| D | HIS25 |
| D | HIS54 |
| D | GLU58 |
| D | HIS73 |
| D | HIS77 |
| D | HIS101 |
| D | ASP106 |
Functional Information from PROSITE/UniProt
| site_id | PS00550 |
| Number of Residues | 24 |
| Details | HEMERYTHRINS Hemerythrin family signature. HFlnEQqlMqasq...Yagyae.HkkaH |
| Chain | Residue | Details |
| A | HIS54-HIS77 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1870128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"678527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1870128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
