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Refined structure of porin from rhodopseudomonas blastica and comparison with the porin from rhodobacter capsulatus

Analyse Refined structure of porin from rhodopseudomonas blastica and comparison with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PRN
Type: protein
Length: 289 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Porin
UniProt: P39767
Pockets: 3 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Porin	protein	289	4% helix, 55% strand	P39767

Ligands and binding sites

C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.37	0.76	29	empty
2	63	0.30	0.75	16	empty
3	55	0.30	0.75	15	empty

Compared structures

1PRN · Refined structure of porin from rhodopseudomonas blastica and comparison with the porin… · the same entry in another collection · chain A against A, TM-score 1.00
P39767 · AlphaFold monomer V2.0 prediction for porin (P39767) · a predicted model of the same protein · 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 P39767
Elsewhere: RCSB PDB 1PRN · PDBe 1PRN · UniProt P39767

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