Research workbench

Fab E8 (FABE8A) X-ray structure at 2.26 ångström resolution

Analyse Fab E8 (FABE8A) X-ray structure at 2.26 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QBL
Type: protein
Length: 433 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FABE8A
UniProt: P01635
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	FABE8A	protein	214	5% helix, 50% strand	P01635
H	FABE8A	protein	219	8% helix, 50% strand	—

Pockets

4 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	564	0.63	0.75	56	empty
2	101	0.41	0.77	19	empty
3	69	0.31	0.75	14	empty
4	56	0.29	0.75	15	empty

Interfaces

1 interface between chains.

L–H · 2102 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

1QBL · Fab E8 (FABE8A) X-ray structure at 2.26 ångström resolution · the same entry in another collection · chain L against L, TM-score 1.00
P01635 · AlphaFold monomer V2.0 prediction for ig kappa chain V-V region K2 (P01635) · a predicted model of the same protein · chain L against A, TM-score 0.44

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 P01635
Elsewhere: RCSB PDB 1QBL · PDBe 1QBL · UniProt P01635

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