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Structure of frmsr

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

PDB: 3RFB
Type: protein
Length: 323 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
EC: 1.8.4.14
UniProt: Q8DQA6
Ligands: SME
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein (EC 1.8.4.14)	protein	160	34% helix, 28% strand	Q8DQA6
B	Putative uncharacterized protein (EC 1.8.4.14)	protein	163	39% helix, 26% strand	Q8DQA6

Ligands and binding sites

SME · Methionine sulfoxide · ligand · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.62	0.90	21	SME

Interfaces

1 interface between chains.

A–B · 1471 Å² buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3RFB · Structure of fRMsr · 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 Q8DQA6
Elsewhere: RCSB PDB 3RFB · PDBe 3RFB · UniProt Q8DQA6

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