MolNFT v1 · #108290 · protein

Biochemical characterization and structural analysis of a new cold- active and salt tolerant esterase from the marine bacterium thalassospira sp

4V2I · ESTERASE/LIPASE: “Biochemical characterization and structural analysis of a new cold- active and salt tolerant esterase from…”. X-ray diffraction, 1 ligand (MG), 4 pockets (best druggability 0.64). MolNFT v1 #108290 on GenesisL1: 3D…

PDB: 4V2I
Type: protein
Length: 630 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ESTERASE/LIPASE
EC: 3.1.1.1
UniProt: A0A023T3X2
Ligands: MG
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ESTERASE/LIPASE (EC 3.1.1.1)	protein	315	42% helix, 20% strand	A0A023T3X2

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

4 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	264	0.64	0.81	38	empty
2	280	0.64	0.80	39	empty
3	180	0.52	0.78	28	empty
4	155	0.49	0.78	28	empty

Interfaces

1 interface between chains.

A–B · 1026 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4V2I · Biochemical characterization and structural analysis of a new cold- active and salt… · 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 A0A023T3X2
Elsewhere: RCSB PDB 4V2I · PDBe 4V2I · UniProt A0A023T3X2

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