MolNFT v1 · #159853 · protein

Crystal structure of the anti-HIV antibody DH501 unmutated common ancestor (uca)

6P3B · DH501UCA Fab heavy chain: “Crystal structure of the anti-HIV antibody DH501 unmutated common ancestor (uca)”. X-ray diffraction, 5 pockets (best druggability 0.58). MolNFT v1 #159853 on GenesisL1: 3D structure, binding sites and…

PDB: 6P3B
Type: protein
Length: 426 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DH501UCA Fab heavy chain; DH501UCA Fab light chain
Pockets: 5 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	DH501UCA Fab heavy chain	protein	214	6% helix, 49% strand	—
L	DH501UCA Fab light chain	protein	212	6% helix, 48% strand	—

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains H, L

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

Pockets

5 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	458	0.58	0.74	42	empty
2	103	0.49	0.81	22	empty
3	173	0.46	0.75	30	empty
4	94	0.38	0.76	17	empty
5	87	0.34	0.74	20	empty

Interfaces

1 interface between chains.

H–L · 1726 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6P3B · Crystal structure of the anti-HIV antibody DH501 unmutated common ancestor (UCA) · the same entry in another collection · chain H against H, 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 6P3B · PDBe 6P3B

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.