MolNFT v1 · #25089 · protein

Bound water molecules and conformational stabilization help mediate an antigen-antibody association

1VFA · IGG1-kappa D1.3 fv (light chain): “Bound water molecules and conformational stabilization help mediate an antigen-antibody association”. X-ray diffraction, 1 pocket (best druggability 0.29). MolNFT v1 #25089 on GenesisL1: 3D…

PDB: 1VFA
Type: protein
Length: 224 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: IGG1-kappa D1.3 fv (light chain); IGG1-kappa D1.3 fv (heavy chain)
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	IGG1-kappa D1.3 fv (light chain)	protein	108	3% helix, 49% strand	—
B	IGG1-kappa D1.3 fv (heavy chain)	protein	116	3% helix, 52% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	71	0.29	0.73	19	empty

Interfaces

1 interface between chains.

A–B · 859 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1VFA · Bound water molecules and conformational stabilization help mediate an antigen-antibody… · 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 1VFA · PDBe 1VFA

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