MolNFT v2 · #35704 · protein

Crystal structure of humanized HYHEL-10 fv mutant(HW47Y)-hen lysozyme complex

2EIZ · Anti-lysozyme antibody fv region: “Crystal structure of humanized HYHEL-10 fv mutant(HW47Y)-hen lysozyme complex”. X-ray diffraction at 1.9, 3 pockets (best druggability 0.64). MolNFT v2 #35704 on GenesisL1: 3D structure, binding…

PDB: 2EIZ
Type: protein
Length: 349 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Source: Gallus gallus; Homo sapiens
Molecule: Anti-lysozyme antibody fv region; Lysozyme C
EC: 3.2.1.17
UniProt: P00698
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · resolution 1.9 · 3 distinct chains · 20% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Anti-lysozyme antibody fv region	protein	107	3% helix, 50% strand	—
B	Anti-lysozyme antibody fv region	protein	113	11% helix, 49% strand	—
C	Lysozyme C (EC 3.2.1.17)	protein	129	42% helix, 11% strand	P00698

Pockets

3 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	182	0.64	0.84	30	empty
2	96	0.39	0.76	17	empty
3	56	0.27	0.73	16	empty

Interfaces

3 interfaces between chains.

A–B · 705 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 545 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 440 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2EIZ · Crystal structure of humanized hyhel-10 fv MUTANT(HW47Y)-hen lysozyme complex · 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 2EIZ · PDBe 2EIZ · UniProt P00698

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