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The crystal structure of carbohydrate acetylesterase family member from sinorhizobium meliloti

Analyse The crystal structure of carbohydrate acetylesterase family member from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TX1
Type: protein
Length: 639 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.2
UniProt: Q7APD5
Pockets: 7 · best druggability 0.70

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Esterase (EC 3.1.1.2)	protein	213	45% helix, 16% strand	Q7APD5

Pockets

7 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	439	0.70	0.81	39	empty
2	421	0.68	0.80	58	empty
3	461	0.66	0.79	43	empty
4	131	0.46	0.77	25	empty
5	69	0.39	0.79	16	empty

Interfaces

3 interfaces between chains.

A–B · 1223 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 457 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 272 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4TX1 · The crystal structure of carbohydrate acetylesterase family member from Sinorhizobium… · 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 Q7APD5
Elsewhere: RCSB PDB 4TX1 · PDBe 4TX1 · UniProt Q7APD5

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