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Crystal structure of the lectin domain of papg from E. COLI BI47 in space group P1

Analyse Crystal structure of the lectin domain of papg from E. COLI BI47 in space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Z3J
Type: protein
Length: 783 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Papg, lectin domain
UniProt: T7DCJ2
Pockets: 8 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Papg, lectin domain	protein	196	2% helix, 58% strand	T7DCJ2
D	Papg, lectin domain	protein	195	2% helix, 58% strand	T7DCJ2

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	594	0.68	0.77	58	empty
2	310	0.51	0.73	32	empty
3	140	0.48	0.78	17	empty
4	177	0.46	0.75	21	empty
5	51	0.34	0.79	16	empty

Interfaces

2 interfaces between chains.

C–D · 362 Å² buried · 1 hydrogen bond · protein-protein
A–B · 294 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4Z3J · Crystal structure of the lectin domain of PapG from E. coli BI47 in space group P1 · 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 T7DCJ2
Elsewhere: RCSB PDB 4Z3J · PDBe 4Z3J · UniProt T7DCJ2

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