MolNFT v1 · #63495 · protein

Crystal structure of a putative arginate lyase from staphylococcus haemolyticus

3FBG: “Crystal structure of a putative arginate lyase from staphylococcus haemolyticus”. X-ray diffraction, 1 ligand (MG), 6 pockets (best druggability 0.76). MolNFT v1 #63495 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3FBG
Type: protein
Length: 668 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative arginate lyase
UniProt: Q4L864
Ligands: MG
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative arginate lyase	protein	336	33% helix, 26% strand	Q4L864
B	Putative arginate lyase	protein	332	33% helix, 26% strand	Q4L864

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	503	0.76	0.84	51	empty
2	526	0.75	0.83	51	empty
3	445	0.59	0.75	42	MG
4	74	0.39	0.78	16	empty
5	55	0.39	0.81	15	empty

Interfaces

1 interface between chains.

A–B · 1359 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

3FBG · Crystal structure of a putative arginate lyase from Staphylococcus haemolyticus · 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 Q4L864
Elsewhere: RCSB PDB 3FBG · PDBe 3FBG · UniProt Q4L864

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