MolNFT v1 · #1078 · protein

Three-dimensional structure of a human Fab with high affinity for tetanus toxoid

1AQK · Fab B7-15A2: “Three-dimensional structure of a human Fab with high affinity for tetanus toxoid”. X-ray diffraction, 5 pockets (best druggability 0.62). MolNFT v1 #1078 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1AQK
Type: protein
Length: 442 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab B7-15A2
UniProt: P01842, P01857
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	Fab B7-15A2	protein	216	8% helix, 48% strand	P01842
H	Fab B7-15A2	protein	226	7% helix, 49% strand	P01857

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.62	0.91	16	empty
2	211	0.52	0.76	26	empty
3	89	0.37	0.76	23	empty
4	80	0.32	0.74	21	empty
5	59	0.27	0.73	16	empty

Interfaces

1 interface between chains.

L–H · 1856 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide, 2 modified (disulfide, cyclization).

Compared structures

1AQK · Three-dimensional structure of a human Fab with high affinity for tetanus toxoid · the same entry in another collection · chain L against L, 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
Every structure of UniProt P01842
Every structure of UniProt P01857
Elsewhere: RCSB PDB 1AQK · PDBe 1AQK · UniProt P01842 · UniProt P01857

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