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Structure of the E. COLI ivy protein

Analyse Structure of the E. COLI ivy protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XS0
Type: protein
Length: 384 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inhibitor of vertebrate lysozyme
UniProt: P45502
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 26% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inhibitor of vertebrate lysozyme	protein	128	27% helix, 34% strand	P45502
B	Inhibitor of vertebrate lysozyme	protein	127	26% helix, 32% strand	P45502
C	Inhibitor of vertebrate lysozyme	protein	129	26% helix, 33% strand	P45502

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	454	0.70	0.81	50	empty
2	63	0.37	0.79	12	empty
3	64	0.36	0.78	17	empty

Interfaces

2 interfaces between chains.

B–C · 958 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 463 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1XS0 · Structure of the E. coli Ivy protein · 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 P45502
Elsewhere: RCSB PDB 1XS0 · PDBe 1XS0 · UniProt P45502

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