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Crystal structure of carf

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

PDB: 5AOH
Type: protein
Length: 526 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spore coat protein coth
UniProt: A0A2I5TIN5
Ligands: K
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spore coat protein coth	protein	265	21% helix, 22% strand	A0A2I5TIN5
B	Spore coat protein coth	protein	261	20% helix, 22% strand	A0A2I5TIN5

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A, 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	502	0.76	0.84	51	empty
2	183	0.44	0.74	26	empty

Interfaces

1 interface between chains.

A–B · 480 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5AOH · Crystal Structure of CarF · 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 A0A2I5TIN5
Elsewhere: RCSB PDB 5AOH · PDBe 5AOH · UniProt A0A2I5TIN5

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