MolNFT v1 · #135867 · protein

ATPase domain of I-aaa protease from myceliophthora thermophila

5UBV: “ATPase domain of I-aaa protease from myceliophthora thermophila”. X-ray diffraction, 1 ligand (ADP), 2 pockets (best druggability 0.74). MolNFT v1 #135867 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5UBV
Type: protein
Length: 482 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATPase domain of I-aaa protease
UniProt: G2QPI5
Ligands: ADP
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATPase domain of I-aaa protease	protein	244	50% helix, 13% strand	G2QPI5
B	ATPase domain of I-aaa protease	protein	238	49% helix, 14% strand	G2QPI5

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
CIT · Citric acid · additive · chains A, B
GOL · Glycerol · additive · chains A, B

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

Pockets

2 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	809	0.74	0.78	85	ADP
2	127	0.47	0.78	29	ADP

Interfaces

1 interface between chains.

A–B · 733 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

5UBV · ATPase domain of i-AAA protease from Myceliophthora thermophila · 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 G2QPI5
Elsewhere: RCSB PDB 5UBV · PDBe 5UBV · UniProt G2QPI5

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