MolNFT v1 · #178978 · protein

The structure of CBM51-2 in complex with glcnac and int domains from clostridium perfringens zmpb

7JRL · F5/8 type C domain protein: “The structure of CBM51-2 in complex with glcnac and int domains from clostridium perfringens zmpb”. X-ray diffraction, 3 ligands (NAG, CA, PO4), 2 pockets (best druggability 0.41). MolNFT v1 #178978 on…

PDB: 7JRL
Type: protein
Length: 457 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: F5/8 type C domain protein
UniProt: A0A0H2YN38
Ligands: NAG, CA, PO4
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	F5/8 type C domain protein	protein	457	18% helix, 40% strand	A0A0H2YN38

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
CA · Calcium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	99	0.41	0.77	20	empty
2	93	0.33	0.73	16	empty

Compared structures

7JRL · The structure of CBM51-2 in complex with GlcNAc and INT domains from Clostridium… · 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
Every structure of UniProt A0A0H2YN38
Elsewhere: RCSB PDB 7JRL · PDBe 7JRL · UniProt A0A0H2YN38

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