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Crystal structure of rffh

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

PDB: 1MC3
Type: protein
Length: 582 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-1-phosphate thymidylyltransferase
EC: 2.7.7.24
UniProt: P61887
Ligands: TTP, MG
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24)	protein	291	36% helix, 22% strand	P61887

Ligands and binding sites

TTP · Thymidine-5'-triphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	921	0.74	0.77	84	MG, TTP
2	886	0.73	0.77	84	MG, TTP
3	209	0.62	0.82	33	empty
4	182	0.54	0.79	25	empty

Interfaces

1 interface between chains.

A–B · 1060 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

1MC3 · Crystal structure of rffh · the same entry in another collection · chain A against A, TM-score 1.00
P61887 · AlphaFold monomer V2.0 prediction for glucose-1-phosphate thymidylyltransferase 2 (P61887) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

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Every structure of UniProt P61887
Elsewhere: RCSB PDB 1MC3 · PDBe 1MC3 · UniProt P61887

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