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The structure of cht

Analyse The structure of cht in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A03
Type: protein
Length: 987 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: M32 carboxypeptidase
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 69% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	M32 carboxypeptidase	protein	493	69% helix, 3% strand	—
B	M32 carboxypeptidase	protein	494	69% helix, 3% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 6 copies · chains A, B
CIT · Citric acid · additive · 2 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · chains A

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

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	1071	0.76	0.78	93	empty
2	614	0.69	0.78	59	empty
3	447	0.66	0.79	42	GOL
4	106	0.48	0.80	24	empty
5	145	0.46	0.77	26	empty

Interfaces

1 interface between chains.

A–B · 1558 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

7A03 · The Structure of CHT · 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
Elsewhere: RCSB PDB 7A03 · PDBe 7A03

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