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Crystal structure of E. COLI lsrf

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

PDB: 3GKF
Type: protein
Length: 5,520 residues
Chains: 20
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldolase lsrf
EC: 4.1.2.-
UniProt: P76143
Pockets: 20 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
O, L, M, N, K, F, I, H, G, J, S, P, Q, R, T, E, B, C, D, A	Aldolase lsrf (EC 4.1.2.-)	protein	276	44% helix, 14% strand	P76143

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	874	0.70	0.76	102	empty
2	51	0.69	0.97	17	empty
3	508	0.64	0.77	76	empty
4	157	0.63	0.85	27	empty
5	156	0.62	0.85	27	empty

Interfaces

39 interfaces between chains.

J–E · 2108 Å² buried · 35 hydrogen bonds · protein-protein
I–D · 2103 Å² buried · 36 hydrogen bonds · protein-protein
F–A · 2101 Å² buried · 35 hydrogen bonds · protein-protein
H–C · 2079 Å² buried · 34 hydrogen bonds · protein-protein
G–B · 2064 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

3GKF · Crystal Structure of E. coli LsrF · 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 P76143
Elsewhere: RCSB PDB 3GKF · PDBe 3GKF · UniProt P76143

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