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Central fibronectin-III array of rim-binding protein

Analyse Central fibronectin-III array of rim-binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q9M
Type: protein
Length: 524 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rim-binding protein, isoform F
UniProt: A0A0B4JDC9
Ligands: PO4
Pockets: 8 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rim-binding protein, isoform F	protein	255	1% helix, 48% strand	A0A0B4JDC9
B	Rim-binding protein, isoform F	protein	269	2% helix, 49% strand	A0A0B4JDC9

Ligands and binding sites

PO4 · Phosphate ion · ion

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

Pockets

8 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	328	0.59	0.78	34	empty
2	166	0.50	0.77	24	empty
3	161	0.43	0.74	28	empty
4	97	0.41	0.77	22	empty
5	91	0.37	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 283 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6Q9M · Central Fibronectin-III array of RIM-binding protein · 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 A0A0B4JDC9
Elsewhere: RCSB PDB 6Q9M · PDBe 6Q9M · UniProt A0A0B4JDC9

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