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Crystal structure of the head-binding domain of phage P22 tailspike protein

Analyse Crystal structure of the head-binding domain of phage P22 tailspike protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LKT
Type: protein
Length: 624 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tailspike protein
UniProt: P12528
Pockets: 8 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Tailspike protein	protein	104	3% helix, 38% strand	P12528

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	429	0.67	0.79	46	empty
2	395	0.64	0.78	35	empty
3	274	0.54	0.76	36	empty
4	149	0.49	0.78	22	empty
5	124	0.48	0.79	21	empty

Interfaces

7 interfaces between chains.

B–C · 1203 Å² buried · 15 hydrogen bonds · protein-protein
E–F · 1185 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 1183 Å² buried · 17 hydrogen bonds · protein-protein
D–E · 1174 Å² buried · 16 hydrogen bonds · protein-protein
D–F · 1165 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

1LKT · Crystal structure of the head-binding domain of phage P22 tailspike protein · the same entry in another collection · chain C against C, 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 P12528
Elsewhere: RCSB PDB 1LKT · PDBe 1LKT · UniProt P12528

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