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Structural basis for zymogen activation and substrate binding of transglutaminase from streptomyces mobaraense

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PDB: 3IU0
Type: protein
Length: 354 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-glutamine gamma-glutamyltransferase
EC: 2.3.2.13
UniProt: P81453
Pockets: 5 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13)	protein	354	36% helix, 16% strand	P81453

Pockets

5 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	50	0.50	0.88	18	empty
2	87	0.45	0.80	22	empty
3	57	0.38	0.80	13	empty
4	76	0.37	0.77	13	empty
5	62	0.32	0.76	17	empty

Compared structures

3IU0 · Structural basis for zymogen activation and substrate binding of transglutaminase from… · the same entry in another collection · chain A against A, TM-score 1.00
P81453 · AlphaFold monomer V2.0 prediction for protein-glutamine gamma- glutamyltransferase… · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt P81453
Elsewhere: RCSB PDB 3IU0 · PDBe 3IU0 · UniProt P81453

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