Research workbench
Crystal structure of the N-terminal bah domain of ORC1P
Analyse Crystal structure of the N-terminal bah domain of ORC1P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M4Z
- Type
- protein
- Length
- 406 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Origin recognition complex subunit 1
- UniProt
- P54784
- Ligands
- MN
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Origin recognition complex subunit 1 | protein | 203 | 31% helix, 35% strand | P54784 |
| B | Origin recognition complex subunit 1 | protein | 203 | 29% helix, 34% strand | P54784 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1140 | 0.80 | 0.82 | 111 | MN |
| 2 | 470 | 0.76 | 0.84 | 51 | empty |
| 3 | 132 | 0.41 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 888 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1M4Z · Crystal structure of the N-terminal BAH domain of Orc1p · the same entry in another collection · chain A against A, TM-score 1.00
- P54784 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 1 (P54784) · a predicted model of the same protein · chain B against A, TM-score 0.91
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 P54784
- Elsewhere: RCSB PDB 1M4Z · PDBe 1M4Z · UniProt P54784
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