MolNFT v1 · #89426 · protein

Structure of free mouse ORC1 bah domain

4DOV · Origin recognition complex subunit 1: “Structure of free mouse ORC1 bah domain”. X-ray diffraction, 2 pockets (best druggability 0.60). MolNFT v1 #89426 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4DOV
Type: protein
Length: 311 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Origin recognition complex subunit 1
UniProt: Q9Z1N2
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Origin recognition complex subunit 1	protein	157	6% helix, 46% strand	Q9Z1N2
C	Origin recognition complex subunit 1	protein	154	8% helix, 46% strand	Q9Z1N2

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	546	0.60	0.73	47	empty
2	51	0.29	0.75	10	empty

Interfaces

1 interface between chains.

A–C · 443 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

4DOV · Structure of free mouse ORC1 BAH domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9Z1N2 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 1 (Q9Z1N2) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q9Z1N2
Elsewhere: RCSB PDB 4DOV · PDBe 4DOV · UniProt Q9Z1N2

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