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Evidence for a dual role of an active site histidine in alpha-amino- beta-carboxymuconate-epsilon-semialdehyde decarboxylase

Analyse Evidence for a dual role of an active site histidine in alpha-amino… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ERA
Type: protein
Length: 664 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase
UniProt: Q83V25
Ligands: CO
Pockets: 4 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	2-amino-3-carboxymuconate 6-semialdehyde decarboxylase	protein	332	45% helix, 16% strand	Q83V25

Ligands and binding sites

CO · Cobalt (II) 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	332	0.58	0.76	39	empty
2	260	0.55	0.76	22	empty
3	63	0.29	0.74	18	empty
4	53	0.26	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 2452 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

4ERA · Evidence for a Dual Role of an Active Site Histidine in… · 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 Q83V25
Elsewhere: RCSB PDB 4ERA · PDBe 4ERA · UniProt Q83V25

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