MolNFT v1 · #90712 · protein

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

4ERG · 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase: “Evidence for a dual role of an active site histidine in alpha-amino…”. X-ray diffraction, 1 ligand (FE), 3 pockets (best druggability 0.62). MolNFT v1 #90712 on GenesisL1: 3D…

PDB: 4ERG
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: FE
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	2-amino-3-carboxymuconate 6-semialdehyde decarboxylase	protein	332	46% helix, 17% strand	Q83V25

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A, B

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

Pockets

3 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	328	0.62	0.78	46	empty
2	316	0.59	0.77	35	empty
3	63	0.38	0.79	18	empty

Interfaces

1 interface between chains.

A–B · 2509 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

4ERG · 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 4ERG · PDBe 4ERG · UniProt Q83V25

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