MolNFT v1 · #49208 · protein

Structure of TA289, a cbs-rubredoxin-like protein, in its FE+2-bound state

2QH1 · Hypothetical protein TA0289: “Structure of TA289, a cbs-rubredoxin-like protein, in its FE+2-bound state”. X-ray diffraction, 1 ligand (FE2), 3 pockets (best druggability 0.78). MolNFT v1 #49208 on GenesisL1: 3D structure, binding…

PDB: 2QH1
Type: protein
Length: 364 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TA0289
UniProt: Q9HLD9
Ligands: FE2
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TA0289	protein	179	33% helix, 27% strand	Q9HLD9
B	Hypothetical protein TA0289	protein	185	33% helix, 26% strand	Q9HLD9

Ligands and binding sites

FE2 · Fe (II) ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	410	0.78	0.87	54	empty
2	135	0.47	0.78	23	empty
3	78	0.41	0.79	19	empty

Interfaces

1 interface between chains.

A–B · 1871 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

2QH1 · Structure of TA289, a CBS-rubredoxin-like protein, in its Fe+2-bound state · 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 Q9HLD9
Elsewhere: RCSB PDB 2QH1 · PDBe 2QH1 · UniProt Q9HLD9

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