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Meta-cleavage product hydrolase from pseudomonas fluorescens IP01 (cumd) S103A mutant hexagonal

Analyse Meta-cleavage product hydrolase from pseudomonas fluorescens IP01 (cumd) S103A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IUN
Type: protein
Length: 548 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Meta-cleavage product hydrolase
EC: 3.7.1.9
UniProt: P96965
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Meta-cleavage product hydrolase (EC 3.7.1.9)	protein	272	42% helix, 18% strand	P96965
B	Meta-cleavage product hydrolase (EC 3.7.1.9)	protein	276	42% helix, 17% strand	P96965

Ligands and binding sites

ACT · Acetate ion · additive · chains A, B

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

Pockets

2 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	203	0.76	0.91	40	empty
2	268	0.75	0.88	52	empty

Interfaces

1 interface between chains.

A–B · 969 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

1IUN · meta-Cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) S103A mutant… · 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 P96965
Elsewhere: RCSB PDB 1IUN · PDBe 1IUN · UniProt P96965

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