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Anti-blood group a fv

Analyse Anti-blood group a fv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JV5
Type: protein
Length: 224 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ig kappa chain precursor V region; Ig chain heavy chain precursor V region
UniProt: P01594
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ig kappa chain precursor V region	protein	107	3% helix, 49% strand	P01594
B	Ig chain heavy chain precursor V region	protein	117	5% helix, 52% strand	—

Pockets

2 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	72	0.43	0.80	14	empty
2	74	0.31	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 766 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1JV5 · Anti-blood group A Fv · the same entry in another collection · chain A against A, TM-score 1.00
P01594 · AlphaFold monomer V2.0 prediction for immunoglobulin kappa variable 1-33 (P01594) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P01594
Elsewhere: RCSB PDB 1JV5 · PDBe 1JV5 · UniProt P01594

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