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Crystal structure of prib

Analyse Crystal structure of prib in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WOC
Type: protein
Length: 397 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Primosomal replication protein N
UniProt: P07013
Pockets: 6 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 69% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Primosomal replication protein N	protein	99	8% helix, 71% strand	P07013
C	Primosomal replication protein N	protein	100	6% helix, 68% strand	P07013

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	365	0.55	0.75	50	empty
2	200	0.55	0.78	29	empty
3	142	0.42	0.75	28	empty
4	54	0.29	0.75	16	empty
5	57	0.28	0.74	12	empty

Interfaces

4 interfaces between chains.

A–D · 1403 Å² buried · 23 hydrogen bonds · protein-protein
B–D · 281 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 174 Å² buried · 1 hydrogen bond · protein-protein
A–C · 21 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

1WOC · Crystal structure of PriB · the same entry in another collection · chain B against B, TM-score 1.00
P07013 · AlphaFold monomer V2.0 prediction for primosomal replication protein N (P07013) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P07013
Elsewhere: RCSB PDB 1WOC · PDBe 1WOC · UniProt P07013

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