Research workbench

Active site SER115ALA mutant of ld-carboxypeptidase

Analyse Active site SER115ALA 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: 2AUM
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: 8 · best druggability 0.69

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, 23% strand	Q9HTZ1

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.69	0.97	17	empty
2	316	0.58	0.77	46	empty
3	275	0.57	0.77	41	empty
4	136	0.44	0.76	19	empty
5	124	0.41	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 1522 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

2AUM · Active site Ser115Ala 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 2AUM · PDBe 2AUM · UniProt Q9HTZ1

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