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Fumarylacetoacetate hydrolase (eafah) from psychrophilic exiguobacterium antarcticum

Analyse Fumarylacetoacetate hydrolase (eafah) from psychrophilic exiguobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IYM
Type: protein
Length: 554 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
UniProt: K0A9N9
Ligands: MG
Pockets: 4 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase	protein	277	17% helix, 34% strand	K0A9N9

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	159	0.50	0.78	32	empty
2	143	0.47	0.77	23	empty
3	125	0.45	0.77	27	empty
4	86	0.35	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1547 Å² buried · 33 hydrogen bonds · protein-protein

Compared structures

6IYM · Fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum · 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 K0A9N9
Elsewhere: RCSB PDB 6IYM · PDBe 6IYM · UniProt K0A9N9

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