MolNFT v1 · #144749 · protein

O2-, plp-dependent L-arginine hydroxylase rohp holoenzyme

6C3B · Uncharacterized protein: “O2-, plp-dependent L-arginine hydroxylase rohp holoenzyme”. X-ray diffraction, 7 pockets (best druggability 0.73). MolNFT v1 #144749 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6C3B
Type: protein
Length: 728 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Uncharacterized protein	protein	364	51% helix, 15% strand	—

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 14 copies · chains A, B
PGE · Triethylene glycol · additive · 3 copies · chains A, B

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

Pockets

7 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	52	0.73	0.99	14	empty
2	313	0.65	0.81	41	EDO, PGE
3	398	0.65	0.79	44	empty
4	174	0.52	0.79	28	empty
5	80	0.37	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 2090 Å² buried · 31 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

6C3B · O2-, PLP-Dependent L-Arginine Hydroxylase RohP Holoenzyme · 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
Elsewhere: RCSB PDB 6C3B · PDBe 6C3B

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