1FFT
The structure of ubiquinol oxidase from Escherichia coli
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, F | UBIQUINOL OXIDASE | polymer | 663 | 74424.5 | 2 | UniProt (P0ABI8) Pfam (PF00115) In PDB | Escherichia coli | |
2 | B, G | UBIQUINOL OXIDASE | polymer | 315 | 34947.2 | 2 | UniProt (P0ABJ1) Pfam (PF00116) Pfam (PF06481) In PDB | Escherichia coli | |
3 | C, H | UBIQUINOL OXIDASE | polymer | 204 | 22642.6 | 2 | UniProt (P0ABJ3) Pfam (PF00510) In PDB | Escherichia coli | |
4 | D, I | UBIQUINOL OXIDASE | polymer | 109 | 9294.4 | 2 | Escherichia coli | ||
5 | A, F | COPPER (II) ION | non-polymer | 63.5 | 2 | Chemie (CU) | |||
6 | A, F | PROTOPORPHYRIN IX CONTAINING FE | non-polymer | 616.5 | 2 | Chemie (HEM) | |||
7 | A, F | HEME O | non-polymer | 838.9 | 2 | Chemie (HEO) |
Sequence modifications
C, H: 25 - 204 (UniProt: P0ABJ3)
PDB | External Database | Details |
---|---|---|
Met 1 | - | cloning artifact |
Ala 2 | - | cloning artifact |
Thr 3 | - | cloning artifact |
Asp 4 | - | cloning artifact |
Thr 5 | - | cloning artifact |
Leu 6 | - | cloning artifact |
Thr 7 | - | cloning artifact |
His 8 | - | cloning artifact |
Ala 9 | - | cloning artifact |
Thr 10 | - | cloning artifact |
Ala 11 | - | cloning artifact |
His 12 | - | cloning artifact |
Ala 13 | - | cloning artifact |
His 14 | - | cloning artifact |
Glu 15 | - | cloning artifact |
His 16 | - | cloning artifact |
Gly 17 | - | cloning artifact |
His 18 | - | cloning artifact |
His 19 | - | cloning artifact |
Asp 20 | - | cloning artifact |
Ala 21 | - | cloning artifact |
Gly 22 | - | cloning artifact |
Gly 23 | - | cloning artifact |
Thr 24 | - | cloning artifact |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 8 |
Total formula weight | 282617.4 | |
Non-Polymers* | Number of molecules | 6 |
Total formula weight | 3037.8 | |
All* | Total formula weight | 285655.1 |