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The crystal structure of a humanized antibody fv 528

Analyse The crystal structure of a humanized antibody fv 528 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WT5
Type: protein
Length: 452 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anti EGFR antibody fv region
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Anti EGFR antibody fv region	protein	115	5% helix, 49% strand	—
C, D	Anti EGFR antibody fv region	protein	111	3% helix, 46% strand	—

Pockets

7 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	966	0.76	0.79	117	empty
2	112	0.41	0.76	27	empty
3	93	0.41	0.77	16	empty
4	110	0.38	0.75	20	empty
5	103	0.37	0.75	18	empty

Interfaces

5 interfaces between chains.

B–D · 830 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 779 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 306 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 159 Å² buried · 1 hydrogen bond · protein-protein
A–D · 152 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1WT5 · The Crystal Structure Of A Humanized Antibody Fv 528 · 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 1WT5 · PDBe 1WT5

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