1UW9: L290F-A222T chlamydomonas Rubisco mutant

L290F-A222T chlamydomonas Rubisco mutant. Determined by X-ray diffraction at 2.05 Å resolution. Released 12 Jan 2005.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: CHLAMYDOMONAS REINHARDTII
Chains: 16
Atoms: 41,674
Mol. weight: 558.9 kDa
Ligands: MG, CAP
Released: 12 Jan 2005

Explore 1UW9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1UW9 contains 268 α-helices and 256 β-strands across 16 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, E, H and V: 28 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	21-24	4
β-strand	25	1	1
α-helix	29-32	4
β-strand	36-44	9	1
α-helix	45	1
α-helix	50-60	11
α-helix	70-74	5
α-helix	77-80	4
β-strand	83-89	7	1
α-helix	90	1
β-strand	97-103	7	1
α-helix	105-107	3
α-helix	113-121	9
α-helix	124-126	3
β-strand	127	1	2
β-strand	130-139	10	1
α-helix	142-145	4
α-helix	155-162	8
β-strand	169-171	3	3
β-strand	173	1	4
α-helix	182-194	13
β-strand	199-201	3	4
β-strand	209	1	5
β-strand	212	1	5
α-helix	214-232	19
β-strand	237-239	3	4
β-strand	240-241	2	3
α-helix	247-260	14
β-strand	264-268	5	3
α-helix	269-272	4
α-helix	274-287	14
β-strand	290-294	5	3
α-helix	298-302	5
β-strand	308-309	2	1
α-helix	311-321	11
β-strand	325-327	3	3
β-strand	335	1	6
α-helix	339-350	12
β-strand	353-354	2	7
β-strand	357	1	8
α-helix	358-360	3
β-strand	362	1	8
β-strand	366-367	2	7
α-helix	371-374	4
β-strand	375-379	5	3
α-helix	384-386	3
α-helix	387-394	8
β-strand	399-401	3	3
α-helix	404-407	4
α-helix	413-432	20
α-helix	437-449	13
α-helix	453-462	10

Chains B, K, O and R: 27 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	21-24	4
β-strand	25	1	9
β-strand	36-44	9	9
α-helix	45	1
α-helix	50-60	11
α-helix	70-74	5
α-helix	77-80	4
β-strand	83-89	7	9
α-helix	90	1
β-strand	97-103	7	9
α-helix	105-107	3
α-helix	113-121	9
α-helix	124-126	3
β-strand	127	1	6
β-strand	130-139	10	9
α-helix	142-145	4
α-helix	155-162	8
β-strand	169-171	3	10
β-strand	173	1	11
α-helix	182-194	13
β-strand	199-201	3	11
β-strand	209	1	12
β-strand	212	1	12
α-helix	214-232	19
β-strand	237-239	3	11
β-strand	240-241	2	10
α-helix	247-260	14
β-strand	264-268	5	10
α-helix	269-272	4
α-helix	274-287	14
β-strand	290-294	5	10
α-helix	298-302	5
β-strand	308-309	2	9
α-helix	311-321	11
β-strand	325-327	3	10
β-strand	335	1	2
α-helix	339-350	12
β-strand	353-354	2	13
β-strand	357	1	14
α-helix	358-360	3
β-strand	362	1	14
β-strand	366-367	2	13
α-helix	371-374	4
β-strand	375-379	5	10
α-helix	384-386	3
α-helix	387-394	8
β-strand	399-401	3	10
α-helix	404-407	4
α-helix	413-432	20
α-helix	437-449	13
α-helix	453-462	10

Chains C, F, I, J, M, P, T and W: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	15
α-helix	20-22	3
α-helix	23-35	13
β-strand	39-45	7	16
α-helix	47-49	3
β-strand	53	1	17
α-helix	55-59	5
β-strand	69	1	17
β-strand	74-76	3	16
α-helix	86-99	14
β-strand	104-111	8	16
β-strand	116-124	9	16
α-helix	135-137	3
β-strand	139	1	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ribulose bisphosphate carboxylase large chain	A, B, E, H, K, O, R, V	protein	475	CHLAMYDOMONAS REINHARDTII	P00877 (AlphaFold model)
Ribulose bisphosphate carboxylase small chain 1	C, F, I, J, M, P, T, W	protein	140	CHLAMYDOMONAS REINHARDTII	P00873 (AlphaFold model)

Sequence of entity 1 (A, B, E, H, K, O, R, V), FASTA

>1UW9_1 RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN (chains A, B, E, H, K, O, R, V)
MVPQTETKAGAGFKAGVKDYRLTYYTPDYVVRDTDILAAFRMTPQPGVPPEECGAAVAAE
SSTGTWTTVWTDGLTSLDRYKGRCYDIEPVPGEDNQYIAYVAYPIDLFEEGSVTNMFTSI
VGNVFGFKALRALRLEDLRIPPAYVKTFVGPPHGIQVERDKLNKYGRGLLGCTIKPKLGL
SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVTEAIYKAQAETGEVKGHYL
NATAGTCEEMMKRAVCAKELGVPIIMHDYLTGGFTANTSLAIYCRDNGLFLHIHRAMHAV
IDRQRNHGIHFRVLAKALRMSGGDHLHSGTVVGKLEGEREVTLGFVDLMRDDYVEKDRSR
GIYFTQDWCSMPGVMPVASGGIHVWHMPALVEIFGDDACLQFGGGTLGHPWGNAPGAAAN
RVALEACTQARNEGRDLAREGGDVIRSACKWSPELAAACEVWKEIKFEFDTIDKL

Sequence of entity 2 (C, F, I, J, M, P, T, W), FASTA

>1UW9_2 RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1 (chains C, F, I, J, M, P, T, W)
MMVWTPVNNKMFETFSYLPPLTDEQIAAQVDYIVANGWIPCLEFAEADKAYVSNESAIRF
GSVSCLYYDNRYWTMWKLPMFGCRDPMQVLREIVACTKAFPDAYVRLVAFDNQKQVQIMG
FLVQRPKSARDWQPANKRSV

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	8
CAP	2-carboxyarabinitol-1,5-diphosphate	C6 H14 O13 P2	8

Water and common crystallization additives (EDO) are not listed.

Primary citation

Altered Intersubunit Interactions in Crystal Structures of Catalytically Compromised Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase. Karkehabadi, S., Taylor, T.C., Spreitzer, R.J. et al. Biochemistry (2005) 44:113. DOI 10.1021/BI047928E · PubMed

Other PDB entries of the same protein (UniProt P00877 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1GK8 1.4 Å, Rubisco from Chlamydomonas reinhardtii
2V6A 1.5 Å, Crystal structure of Chlamydomonas reinhardtii Rubisco with large- subunit mutations…
2V63 1.8 Å, Crystal structure of Rubisco from Chlamydomonas reinhardtii with a large-subunit V331A…
1IR2 1.84 Å, Crystal Structure of Activated Ribulose-1,5-bisphosphate Carboxylase/oxygenase (Rubisco)…
5BS2 1.97 Å, Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL…
2V67 2.0 Å, Crystal structure of Chlamydomonas reinhardtii Rubisco with a large- subunit supressor…
7JSX 2.06 Å, EPYC1(106-135) peptide-bound Rubisco
7JFO 2.13 Å, EPYC1(49-72)-bound Rubisco
1UZH 2.2 Å, A chimeric chlamydomonas, synechococcus rubisco enzyme
1UWA 2.3 Å, L290F mutant rubisco from chlamydomonas
2V68 2.3 Å, Crystal structure of Chlamydomonas reinhardtii Rubisco with large- subunit mutations…
2VDH 2.3 Å, Crystal structure of Chlamydomonas reinhardtii Rubisco with a large- subunit C172S…

Browse structure collections

About this viewer

MolViewer shows 1UW9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.