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Solution structure of PH1500: a homohexameric protein centered on a 12-bladed beta-propeller

Analyse Solution structure of PH1500: a homohexameric protein centered on a 12-bladed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2M3X
Type: protein
Length: 882 residues
Chains: 6
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PH1500
UniProt: O59169
Pockets: 9 · best druggability 0.65

Structure

solution nmr · 1 distinct chain · 6% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	PH1500	protein	147	6% helix, 54% strand	O59169

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.65	0.94	19	empty
2	65	0.61	0.90	19	empty
3	79	0.57	0.86	19	empty
4	67	0.57	0.88	22	empty
5	62	0.56	0.88	16	empty

Interfaces

6 interfaces between chains.

B–C · 1092 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 1063 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 1047 Å² buried · 14 hydrogen bonds · protein-protein
E–F · 1044 Å² buried · 15 hydrogen bonds · protein-protein
D–E · 988 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2M3X · Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed… · 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 O59169
Elsewhere: RCSB PDB 2M3X · PDBe 2M3X · UniProt O59169

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