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Crystal structure of the BCR Fab fragment from subset #4 case CLL183

Analyse Crystal structure of the BCR Fab fragment from subset #4 case CLL183 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DRW
Type: protein
Length: 436 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.27
Source: Homo sapiens
Molecule: CLL183 BCR antibody heavy chain; CLL183 BCR antibody light chain
Pockets: 4 · best druggability 0.47

Structure

x-ray diffraction · resolution 2.27 · 2 distinct chains · 6% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CLL183 BCR antibody heavy chain	protein	218	8% helix, 52% strand	—
B	CLL183 BCR antibody light chain	protein	218	5% helix, 50% strand	—

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	232	0.47	0.74	37	empty
2	85	0.31	0.73	17	empty
3	50	0.26	0.74	13	empty
4	52	0.26	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 1919 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5DRW · Crystal structure of the BCR Fab fragment from subset #4 case CLL183 · 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
Elsewhere: RCSB PDB 5DRW · PDBe 5DRW

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