MolNFT v1 · #139912 · protein

Complex structure of RMMAN134A-M4

5XU5 · Endo-1,4-beta-mannanase: “Complex structure of RMMAN134A-M4”. X-ray diffraction, 1 ligand (BMA), 5 pockets (best druggability 0.49). MolNFT v1 #139912 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5XU5
Type: protein
Length: 320 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-mannanase
UniProt: A0A0A1NDE2
Ligands: BMA
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Endo-1,4-beta-mannanase	protein	160	63% helix, 9% strand	A0A0A1NDE2

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · 8 copies · chains B, A

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

Pockets

5 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	225	0.49	0.75	40	empty
2	131	0.42	0.76	23	BMA
3	102	0.37	0.75	19	BMA
4	60	0.35	0.78	17	empty
5	54	0.28	0.74	11	empty

Interfaces

1 interface between chains.

B–A · 684 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5XU5 · Complex structure of RmMan134A-M4 · 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 A0A0A1NDE2
Elsewhere: RCSB PDB 5XU5 · PDBe 5XU5 · UniProt A0A0A1NDE2

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