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Crystal structure of CUTA1 from oryza sativa

Analyse Crystal structure of CUTA1 from oryza sativa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZOM
Type: protein
Length: 324 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein cuta, chloroplast, putative, expressed
UniProt: Q109R6
Ligands: SO4
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein cuta, chloroplast, putative, expressed	protein	107	34% helix, 38% strand	Q109R6
B	Protein cuta, chloroplast, putative, expressed	protein	108	31% helix, 37% strand	Q109R6
C	Protein cuta, chloroplast, putative, expressed	protein	109	30% helix, 40% strand	Q109R6

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
GOL · Glycerol · additive · 3 copies · chains A, B, C

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

Pockets

3 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	154	0.57	0.81	17	empty
2	115	0.56	0.83	16	empty
3	124	0.53	0.81	15	empty

Interfaces

3 interfaces between chains.

B–C · 1096 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 1051 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1041 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

2ZOM · Crystal structure of CutA1 from Oryza sativa · the same entry in another collection · chain A against A, TM-score 1.00
Q109R6 · AlphaFold monomer V2.0 prediction for protein cuta 1, chloroplastic (Q109R6) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 Q109R6
Elsewhere: RCSB PDB 2ZOM · PDBe 2ZOM · UniProt Q109R6

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