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Structure of a domain of an uncharacterized protein PG_1388 from porphyromonas gingivalis W83

Analyse Structure of a domain of an uncharacterized protein PG_1388 from porphyromonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P3P
Type: protein
Length: 395 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
UniProt: Q7MUU3
Ligands: MG
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein	protein	197	22% helix, 34% strand	Q7MUU3
B	Hypothetical protein	protein	198	24% helix, 35% strand	Q7MUU3

Ligands and binding sites

MG · Magnesium ion · metal · chains B

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

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	734	0.72	0.78	72	empty
2	63	0.35	0.77	15	MG

Interfaces

1 interface between chains.

A–B · 717 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2P3P · Structure of a domain of an uncharacterized protein PG_1388 from Porphyromonas gingivalis… · 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 Q7MUU3
Elsewhere: RCSB PDB 2P3P · PDBe 2P3P · UniProt Q7MUU3

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