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Structure of udp-galactopyranose mutase from klebsiella pneumoniae with fadh-

Analyse Structure of udp-galactopyranose mutase from klebsiella pneumoniae with fadh- in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WAM
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-galactopyranose mutase
EC: 5.4.99.9
UniProt: Q48485
Ligands: FAD
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-galactopyranose mutase (EC 5.4.99.9)	protein	377	32% helix, 23% strand	Q48485

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1133	0.79	0.81	91	FAD

Compared structures

1WAM · Structure of UDP-galactopyranose mutase from Klebsiella Pneumoniae with FADH- · the same entry in another collection · chain A against A, TM-score 1.00
Q48485 · AlphaFold monomer V2.0 prediction for udp-galactopyranose mutase (Q48485) · a predicted model of the same protein · 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 Q48485
Elsewhere: RCSB PDB 1WAM · PDBe 1WAM · UniProt Q48485

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