7BH2
Cryo-EM Structure of KdpFABC in E2Pi state with BeF3 and K+
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Potassium-transporting ATPase potassium-binding subunit | polymer | 557 | 59247.7 | 1 | UniProt (P03959) Pfam (PF03814) | Escherichia coli K-12 | ATP phosphohydrolase [potassium-transporting] A chain,Potassium-binding and translocating subunit A,Potassium-translocating ATPase A chain |
| 2 | B (B) | Potassium-transporting ATPase ATP-binding subunit | polymer | 682 | 72251.9 | 1 | UniProt (P03960) Pfam (PF00122) Pfam (PF00702) | Escherichia coli K-12 | ATP phosphohydrolase [potassium-transporting] B chain,Potassium-binding and translocating subunit B,Potassium-translocating ATPase B chain |
| 3 | C (C) | Potassium-transporting ATPase KdpC subunit | polymer | 208 | 22299.2 | 1 | UniProt (P03961) Pfam (PF02669) | Escherichia coli K-12 | ATP phosphohydrolase [potassium-transporting] C chain,Potassium-binding and translocating subunit C,Potassium-translocating ATPase C chain |
| 4 | D (D) | Potassium-transporting ATPase KdpF subunit | polymer | 29 | 3071.7 | 1 | UniProt (P36937) Pfam (PF09604) | Escherichia coli K-12 | ATP phosphohydrolase [potassium-transporting] F chain,Potassium-binding and translocating subunit F,Potassium-translocating ATPase F chain |
| 5 | E, F (A) | POTASSIUM ION | non-polymer | 39.1 | 2 | Chemie (K) | |||
| 6 | G (B) | (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate | non-polymer | 718.0 | 1 | Chemie (9Y0) | |||
| 7 | H (B) | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
| 8 | I (B) | BERYLLIUM TRIFLUORIDE ION | non-polymer | 66.0 | 1 | Chemie (BEF) | |||
| 9 | J, K, L (A, B, D) | water | water | 18.0 | 13 | Chemie (HOH) |
Sequence modifications
A: 1 - 557 (UniProt: P03959)
B: 1 - 682 (UniProt: P03960)
C: 1 - 190 (UniProt: P03961)
| PDB | External Database | Details |
|---|---|---|
| Arg 116 | Gln 116 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Ala 162 | Ser 162 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Gly 191 | - | expression tag |
| Thr 192 | - | expression tag |
| Gly 193 | - | expression tag |
| Leu 194 | - | expression tag |
| Val 195 | - | expression tag |
| Pro 196 | - | expression tag |
| Arg 197 | - | expression tag |
| Gly 198 | - | expression tag |
| Ser 199 | - | expression tag |
| Ser 200 | - | expression tag |
| His 201 | - | expression tag |
| His 202 | - | expression tag |
| His 203 | - | expression tag |
| His 204 | - | expression tag |
| His 205 | - | expression tag |
| His 206 | - | expression tag |
| His 207 | - | expression tag |
| His 208 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 156870.5 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 886.5 | |
| All* | Total formula weight | 157757.0 |
