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Crystal structure of an ancient sequence-reconstructed elongation factor tu (node 184)

Analyse Crystal structure of an ancient sequence-reconstructed elongation factor tu… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HTW
Type: protein
Length: 741 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor tu
Ligands: GDP, MG
Pockets: 6 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Elongation factor tu	protein	356	23% helix, 39% strand	—
B	Elongation factor tu	protein	385	23% helix, 38% strand	—

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains H, B
MG · Magnesium ion · metal · 2 copies · chains H, B

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

Pockets

6 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	254	0.64	0.82	43	empty
2	379	0.57	0.75	47	empty
3	419	0.57	0.74	47	empty
4	99	0.39	0.76	16	empty
5	75	0.34	0.76	19	GDP, MG

Interfaces

1 interface between chains.

H–B · 596 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6HTW · Crystal structure of an ancient sequence-reconstructed Elongation factor Tu (node 184) · the same entry in another collection · chain H against H, 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
Elsewhere: RCSB PDB 6HTW · PDBe 6HTW

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