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Crystal structure of HPV L1-directed D24.M01FAB

Analyse Crystal structure of HPV L1-directed D24.M01FAB in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MU4
Type: protein
Length: 441 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D24.M01 Fab heavy chain; D24.M01 Fab light chain
Pockets: 5 · best druggability 0.67

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	D24.M01 Fab heavy chain	protein	226	7% helix, 50% strand	—
L	D24.M01 Fab light chain	protein	215	7% helix, 50% strand	—

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · 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	611	0.67	0.77	56	empty
2	160	0.48	0.77	22	empty
3	126	0.42	0.76	22	empty
4	86	0.40	0.78	19	empty
5	52	0.33	0.78	15	empty

Interfaces

1 interface between chains.

H–L · 1865 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

7MU4 · Crystal Structure of HPV L1-directed D24.M01Fab · 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 7MU4 · PDBe 7MU4

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