Research workbench

Active site HIS285ALA mutant of ld-carboxypeptidase

Analyse Active site HIS285ALA mutant of ld-carboxypeptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AUN
Type: protein
Length: 588 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
EC: 3.4.17.13
UniProt: Q9HTZ1
Pockets: 7 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein (EC 3.4.17.13)	protein	294	35% helix, 23% strand	Q9HTZ1
B	Hypothetical protein (EC 3.4.17.13)	protein	294	35% helix, 22% strand	Q9HTZ1

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	354	0.61	0.77	46	empty
2	302	0.58	0.77	41	empty
3	141	0.45	0.76	20	empty
4	115	0.41	0.76	21	empty
5	82	0.34	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 1499 Å² buried · 33 hydrogen bonds · protein-protein

Compared structures

2AUN · Active site His285Ala mutant of LD-carboxypeptidase · the same entry in another collection · chain A against A, TM-score 1.00
Q9HTZ1 · AlphaFold monomer V2.0 prediction for murein tetrapeptide carboxypeptidase (Q9HTZ1) · 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 Q9HTZ1
Elsewhere: RCSB PDB 2AUN · PDBe 2AUN · UniProt Q9HTZ1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.