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Crystal structure of a camel single-domain vh antibody fragment in complex with lysozyme

Analyse Crystal structure of a camel single-domain vh antibody fragment in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MEL
Type: protein
Length: 518 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vh single-domain antibody; Lysozyme
EC: 3.2.1.17
UniProt: P00698
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Vh single-domain antibody	protein	132	6% helix, 48% strand	—
L, M	Lysozyme (EC 3.2.1.17)	protein	127	43% helix, 11% strand	P00698

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	217	0.47	0.74	25	empty
2	52	0.31	0.76	14	empty

Interfaces

3 interfaces between chains.

A–L · 879 Å² buried · 13 hydrogen bonds · protein-protein
B–M · 801 Å² buried · 13 hydrogen bonds · protein-protein
L–M · 411 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

1MEL · Crystal structure of a camel single-domain vh antibody fragment in complex with lysozyme · 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
Every structure of UniProt P00698
Elsewhere: RCSB PDB 1MEL · PDBe 1MEL · UniProt P00698

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