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Phage resistance protein

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

PDB: 7P9K
Type: protein
Length: 1,160 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DUF262 domain-containing protein
UniProt: B7L3S9
Ligands: SO4, CL
Pockets: 15 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	DUF262 domain-containing protein	protein	580	50% helix, 10% strand	B7L3S9

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 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	216	0.57	0.79	34	SO4
2	248	0.56	0.77	35	SO4
3	149	0.48	0.78	27	empty
4	166	0.47	0.76	25	empty
5	172	0.47	0.75	23	empty

Interfaces

1 interface between chains.

A–B · 2705 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

7P9K · BrxU, GmrSD-family Type IV restriction enzyme · the same entry in another collection · chain A against A, TM-score 1.00

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 B7L3S9
Elsewhere: RCSB PDB 7P9K · PDBe 7P9K · UniProt B7L3S9

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