MolNFT v1 · #66104 · protein

Universal stress protein tead from the trap transporter teaabc of halomonas elongata

3HGM: “Universal stress protein tead from the trap transporter teaabc of halomonas elongata”. X-ray diffraction, 2 ligands (ATP, MG), 8 pockets (best druggability 0.85). MolNFT v1 #66104 on GenesisL1: 3D structure, binding sites and…

PDB: 3HGM
Type: protein
Length: 570 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Universal stress protein tead
UniProt: D4AEP4
Ligands: ATP, MG
Pockets: 8 · best druggability 0.85

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Universal stress protein tead	protein	147	46% helix, 20% strand	D4AEP4
C	Universal stress protein tead	protein	135	45% helix, 21% strand	D4AEP4
D	Universal stress protein tead	protein	141	43% helix, 21% strand	D4AEP4

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, C, B, D
MG · Magnesium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	829	0.85	0.87	81	ATP, MG
2	818	0.83	0.85	87	ATP, MG
3	115	0.64	0.89	26	empty
4	97	0.58	0.86	18	empty
5	83	0.55	0.86	20	empty

Interfaces

6 interfaces between chains.

B–D · 1503 Å² buried · 20 hydrogen bonds · protein-protein
A–C · 1365 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 888 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 824 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 38 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3HGM · Universal Stress Protein TeaD from the TRAP transporter TeaABC of Halomonas elongata · 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 D4AEP4
Elsewhere: RCSB PDB 3HGM · PDBe 3HGM · UniProt D4AEP4

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