MolNFT v1 · #67093 · protein

Crystal structure of CALG2, calicheamicin glycosyltransferase, tdp bound form

3IAA: “Crystal structure of CALG2, calicheamicin glycosyltransferase, tdp bound form”. X-ray diffraction, 1 ligand (TYD), 5 pockets (best druggability 0.87). MolNFT v1 #67093 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3IAA
Type: protein
Length: 792 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CALG2
UniProt: Q8KNE0
Ligands: TYD
Pockets: 5 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CALG2	protein	396	48% helix, 14% strand	Q8KNE0

Ligands and binding sites

TYD · Thymidine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

5 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	713	0.87	0.91	91	TYD
2	694	0.87	0.91	92	TYD
3	125	0.40	0.75	16	empty
4	98	0.35	0.74	17	empty
5	57	0.27	0.73	20	empty

Interfaces

1 interface between chains.

A–B · 1180 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

3IAA · Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP bound form · the same entry in another collection · chain B against B, 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 Q8KNE0
Elsewhere: RCSB PDB 3IAA · PDBe 3IAA · UniProt Q8KNE0

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