MolNFT v1 · #24469 · protein

L290F-A222T chlamydomonas rubisco mutant

1UW9 · Ribulose bisphosphate carboxylase large chain: “L290F-A222T chlamydomonas rubisco mutant”. X-ray diffraction, 2 ligands (CAP, MG), 20 pockets (best druggability 0.81). MolNFT v1 #24469 on GenesisL1: 3D structure, binding sites and…

PDB: 1UW9
Type: protein
Length: 4,855 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase small…
EC: 4.1.1.39
UniProt: P00877, P00873
Ligands: CAP, MG
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 5 distinct chains · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E, R	Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39)	protein	465	44% helix, 17% strand	P00877
B	Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39)	protein	467	44% helix, 17% strand	P00877
C, F, I, J, M, P, T, W	Ribulose bisphosphate carboxylase small chain 1 (EC 4.1.1.39)	protein	140	27% helix, 22% strand	P00873
H, K, O	Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39)	protein	469	43% helix, 17% strand	P00877
V	Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39)	protein	466	44% helix, 17% strand	P00877

Ligands and binding sites

CAP · 2-carboxyarabinitol-1,5-diphosphate · ligand · 8 copies · chains A, B, E, K, O, V, H, R
MG · Magnesium ion · metal · 8 copies · chains A, B, E, K, H, R, O, V
EDO · 1,2-ethanediol · additive · 55 copies · chains A, B, C, V, E, K, H, R, I, J, M, O, P, T, W

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	131	0.81	0.99	44	CAP, MG, EDO
2	135	0.79	0.97	46	MG, CAP, EDO
3	125	0.79	0.98	43	CAP, MG
4	846	0.78	0.82	55	empty
5	868	0.78	0.81	56	empty

Interfaces

48 interfaces between chains.

A–B · 4825 Å² buried · 92 hydrogen bonds · protein-protein
O–V · 4818 Å² buried · 93 hydrogen bonds · protein-protein
H–R · 4811 Å² buried · 92 hydrogen bonds · protein-protein
E–K · 4800 Å² buried · 92 hydrogen bonds · protein-protein
V–W · 2008 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 40 modified, 3 disulfide (hydroxylation, methylation, carboxylation, disulfide).

Compared structures

1UW9 · L290F-A222T chlamydomonas Rubisco mutant · the same entry in another collection · chain W against W, 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 P00877
Every structure of UniProt P00873
Elsewhere: RCSB PDB 1UW9 · PDBe 1UW9 · UniProt P00877 · UniProt P00873

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