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The crystal structure of methylglyoxal synthase from thermus sp. GH5 bound to phosphate ion.

Analyse The crystal structure of methylglyoxal synthase from thermus sp. GH5 bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XW6
Type: protein
Length: 381 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methylglyoxal synthase
EC: 4.2.3.3
UniProt: B3VH91
Ligands: PO4

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methylglyoxal synthase (EC 4.2.3.3)	protein	130	48% helix, 15% strand	B3VH91
B	Methylglyoxal synthase (EC 4.2.3.3)	protein	127	51% helix, 16% strand	B3VH91
C	Methylglyoxal synthase (EC 4.2.3.3)	protein	124	52% helix, 16% strand	B3VH91

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A, B, C

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

Interfaces

2 interfaces between chains.

A–C · 1004 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 138 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2XW6 · The Crystal Structure of Methylglyoxal Synthase from Thermus sp. GH5 Bound to Phosphate… · 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 B3VH91
Elsewhere: RCSB PDB 2XW6 · PDBe 2XW6 · UniProt B3VH91

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