MolNFT v1 · #136120 · protein
Structure of the active form of human origin recognition complex ATPase motor module, complex subunits 1, 4, 5
5UJ7 · Origin recognition complex subunit 1: “Structure of the active form of human origin recognition complex ATPase motor module, complex subunits 1, 4, 5”. X-ray diffraction, 3 ligands (ATP, MG, K), 20 pockets (best druggability 0.88).…
- PDB
- 5UJ7
- Type
- protein
- Length
- 1,935 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Origin recognition complex subunit 1; Origin recognition complex subunit 4; Origin…
- UniProt
- Q13415, O43929, O43913
- Ligands
- ATP, MG, K
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 5 distinct chains · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Origin recognition complex subunit 1 | protein | 337 | 54% helix, 10% strand | Q13415 |
| C | Origin recognition complex subunit 4 | protein | 394 | 55% helix, 9% strand | O43929 |
| E | Origin recognition complex subunit 5 | protein | 242 | 49% helix, 11% strand | O43913 |
| D | Origin recognition complex subunit 4 | protein | 385 | 56% helix, 10% strand | O43929 |
| F | Origin recognition complex subunit 5 | protein | 240 | 50% helix, 11% strand | O43913 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 6 copies · chains A, C, E, B, D, F
- MG · Magnesium ion · metal · 4 copies · chains A, C, E, B, D, F
- K · Potassium ion · metal · 2 copies · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 665 | 0.88 | 0.93 | 76 | ATP, MG |
| 2 | 508 | 0.87 | 0.93 | 72 | empty |
| 3 | 260 | 0.82 | 0.94 | 40 | ATP, MG |
| 4 | 96 | 0.78 | 0.98 | 20 | empty |
| 5 | 632 | 0.77 | 0.83 | 60 | ATP, MG |
Interfaces
8 interfaces between chains.
- A–C · 2916 Ų buried · 41 hydrogen bonds · protein-protein
- B–D · 2780 Ų buried · 38 hydrogen bonds · protein-protein
- C–E · 2527 Ų buried · 32 hydrogen bonds · protein-protein
- D–F · 2512 Ų buried · 26 hydrogen bonds · protein-protein
- A–E · 488 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5UJ7 · Structure of the active form of human Origin Recognition Complex ATPase motor module… · the same entry in another collection · chain F against F, TM-score 1.00
- Q13415 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 1 (Q13415) · a predicted model of the same protein · chain A against A, TM-score 0.98
- O43913 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 5 (O43913) · a predicted model of the same protein · chain E against A, TM-score 0.98
- O43929 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 4 (O43929) · a predicted model of the same protein · chain D against A, TM-score 0.95
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q13415
- Every structure of UniProt O43929
- Every structure of UniProt O43913
- Elsewhere: RCSB PDB 5UJ7 · PDBe 5UJ7 · UniProt Q13415 · UniProt O43929 · UniProt O43913
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