MolNFT v1 · #148518 · protein

Structure of the family GH92 alpha-mannosidase BT3965 from bacteroides thetaiotaomicron

6F91: “Structure of the family GH92 alpha-mannosidase BT3965 from bacteroides thetaiotaomicron”. X-ray diffraction, 3 ligands (NA, CA, CL). MolNFT v1 #148518 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6F91
Type: protein
Length: 5,928 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: A0A139JT15
Ligands: NA, CA, CL

Structure

x-ray diffraction · 8 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	740	—	A0A139JT15
B	—	protein	738	—	A0A139JT15
C	—	protein	747	—	A0A139JT15
D	—	protein	742	—	A0A139JT15
E	—	protein	742	—	A0A139JT15
F	—	protein	736	—	A0A139JT15
G	—	protein	742	—	A0A139JT15
H	—	protein	741	—	A0A139JT15

Ligands and binding sites

NA · Sodium ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
CA · Calcium ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
CL · Chloride ion · ion · 8 copies · chains A, B, C, D, E, F, G, H
EDO · 1,2-ethanediol · additive · 26 copies · chains A, B, C, D, E, F, G, H

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

Compared structures

6F91 · Structure of the family GH92 alpha-mannosidase BT3965 from Bacteroides thetaiotaomicron · 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 A0A139JT15
Elsewhere: RCSB PDB 6F91 · PDBe 6F91 · UniProt A0A139JT15

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