Research workbench
Human origin recognition complex, ORC1-5 state I
Analyse Human origin recognition complex, ORC1-5 state I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CTG
- Type
- protein
- Length
- 1,775 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Origin recognition complex subunit 1; Origin recognition complex subunit 2; Origin…
- UniProt
- Q13415, Q13416, Q9UBD5, O43929, O43913
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 5 distinct chains · 53% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Origin recognition complex subunit 1 | protein | 102 | 59% helix, 6% strand | Q13415 |
| B | Origin recognition complex subunit 2 | protein | 302 | 44% helix, 10% strand | Q13416 |
| C | Origin recognition complex subunit 3 | protein | 592 | 58% helix, 5% strand | Q9UBD5 |
| D | Origin recognition complex subunit 4 | protein | 406 | 54% helix, 6% strand | O43929 |
| E | Origin recognition complex subunit 5 | protein | 373 | 48% helix, 9% strand | O43913 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.82 | 0.86 | 87 | empty |
| 2 | 575 | 0.82 | 0.87 | 76 | ATP |
| 3 | 550 | 0.81 | 0.87 | 65 | empty |
| 4 | 622 | 0.78 | 0.83 | 69 | ATP |
| 5 | 375 | 0.76 | 0.87 | 51 | empty |
Interfaces
9 interfaces between chains.
- B–C · 2952 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 2725 Ų buried · 18 hydrogen bonds · protein-protein
- C–E · 1836 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1261 Ų buried · 14 hydrogen bonds · protein-protein
- B–E · 991 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7CTG · Human Origin Recognition Complex, ORC1-5 State I · the same entry in another collection · chain E against E, 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 0.99
- Q9UBD5 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 3 (Q9UBD5) · a predicted model of the same protein · chain C against A, TM-score 0.96
- 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 0.94
- 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 0.92
- Q13416 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 2 (Q13416) · a predicted model of the same protein · chain B against A, TM-score 0.66
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 Q13416
- Every structure of UniProt Q9UBD5
- Every structure of UniProt O43929
- Every structure of UniProt O43913
- Elsewhere: RCSB PDB 7CTG · PDBe 7CTG · UniProt Q13415 · UniProt Q13416 · UniProt Q9UBD5 · UniProt O43929 · UniProt O43913
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