MolNFT v1 · #50207 · protein

Gamma-glutamyl cyclotransferase

2RBH: “Gamma-glutamyl cyclotransferase”. X-ray diffraction, 8 pockets (best druggability 0.71). MolNFT v1 #50207 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2RBH
Type: protein
Length: 338 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gamma-glutamyl cyclotransferase
EC: 2.3.2.4
UniProt: O75223
Pockets: 8 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gamma-glutamyl cyclotransferase (EC 2.3.2.4)	protein	169	30% helix, 37% strand	O75223
B	Gamma-glutamyl cyclotransferase (EC 2.3.2.4)	protein	169	30% helix, 37% strand	O75223

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	266	0.71	0.85	38	empty
2	258	0.69	0.85	34	empty
3	158	0.56	0.81	26	empty
4	125	0.54	0.82	22	empty
5	213	0.50	0.76	25	empty

Interfaces

1 interface between chains.

A–B · 866 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

2RBH · Gamma-glutamyl cyclotransferase · the same entry in another collection · chain A against A, TM-score 1.00
O75223 · AlphaFold monomer V2.0 prediction for gamma-glutamylcyclotransferase (O75223) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 O75223
Elsewhere: RCSB PDB 2RBH · PDBe 2RBH · UniProt O75223

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