MolNFT v1 · #172331 · protein

RBCEL1 cellulase variant Y201F with cellotriose covalently bound

6ZZ3 · Endoglucanase: “RBCEL1 cellulase variant Y201F with cellotriose covalently bound”. X-ray diffraction, 2 ligands (BGC, GLC), 11 pockets (best druggability 0.73). MolNFT v1 #172331 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6ZZ3
Type: protein
Length: 1,276 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase
EC: 3.2.1.4
UniProt: C1JI15
Ligands: BGC, GLC
Pockets: 11 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 35% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endoglucanase (EC 3.2.1.4)	protein	319	35% helix, 16% strand	C1JI15
C	Endoglucanase (EC 3.2.1.4)	protein	318	36% helix, 17% strand	C1JI15
D	Endoglucanase (EC 3.2.1.4)	protein	320	35% helix, 16% strand	C1JI15

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D
GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
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

11 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	1016	0.73	0.76	81	empty
2	862	0.69	0.75	67	empty
3	293	0.53	0.75	33	empty
4	130	0.44	0.77	30	GLC, BGC
5	125	0.42	0.76	27	GLC, BGC

Interfaces

5 interfaces between chains.

C–D · 376 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 241 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 159 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 86 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 27 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 4 glycan (disulfide, glycosylation).

Compared structures

6ZZ3 · RBcel1 cellulase variant Y201F with cellotriose covalently bound · the same entry in another collection · chain D against D, 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 C1JI15
Elsewhere: RCSB PDB 6ZZ3 · PDBe 6ZZ3 · UniProt C1JI15

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