1UZD: Chlamydomonas,Spinach Chimeric Rubisco

Chlamydomonas,Spinach Chimeric Rubisco. Determined by X-ray diffraction at 2.4 Å resolution. Released 31 May 2005.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Chlamydomonas reinhardtii, Spinacia oleracea
Chains: 16
Atoms: 40,055
Mol. weight: 553.74 kDa
Ligands: CAP, MG
Released: 31 May 2005

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

Secondary structure: helices and β-sheets

1UZD contains 262 α-helices and 260 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.

Chain A: 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	182-195	14
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	437-451	15
α-helix	453-462	10

Chain B: 28 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	16	1	9
α-helix	21-24	4
β-strand	25	1	10
α-helix	29-32	4
β-strand	36-44	9	10
α-helix	45	1
α-helix	50-60	11
β-strand	68	1	9
α-helix	70-74	5
α-helix	77-80	4
β-strand	83-89	7	10
α-helix	90	1
β-strand	97-103	7	10
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	10
α-helix	142-145	4
α-helix	155-162	8
β-strand	169-171	3	11
β-strand	173	1	12
α-helix	182-194	13
β-strand	199-201	3	12
β-strand	209	1	13
β-strand	212	1	13
α-helix	214-232	19
β-strand	237-239	3	12
β-strand	240-241	2	11
α-helix	247-260	14
β-strand	264-268	5	11
α-helix	269-272	4
α-helix	274-287	14
β-strand	290-294	5	11
α-helix	298-302	5
β-strand	308-309	2	10
α-helix	311-321	11
β-strand	325-327	3	11
β-strand	335	1	2
α-helix	339-350	12
β-strand	353-354	2	14
β-strand	357	1	15
α-helix	358-360	3
β-strand	362	1	15
β-strand	366-367	2	14
α-helix	371-374	4
β-strand	375-379	5	11
α-helix	384-386	3
α-helix	387-394	8
β-strand	399-401	3	11
α-helix	404-407	4
α-helix	413-432	20
α-helix	437-451	15
α-helix	453-462	10

Chains C, F, J, P, T and W: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3	1
β-strand	4	1	16
α-helix	5	1
α-helix	20-22	3
α-helix	23-36	14
β-strand	39-45	7	17
β-strand	52	1	18
β-strand	63	1	18
β-strand	68-70	3	17
α-helix	80-93	14
β-strand	98-105	8	17
β-strand	110-118	9	17
β-strand	133	1	16

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

Element	Residues	Length	Sheet
α-helix	21-24	4
β-strand	25	1	19
α-helix	29-32	4
β-strand	36-44	9	19
α-helix	45	1
α-helix	50-60	11
α-helix	70-74	5
α-helix	77-80	4
β-strand	83-89	7	19
α-helix	90	1
β-strand	97-103	7	19
α-helix	105-107	3
α-helix	113-121	9
α-helix	124-126	3
β-strand	127	1	20
β-strand	130-139	10	19
α-helix	142-145	4
α-helix	155-162	8
β-strand	169-171	3	21
β-strand	173	1	22
α-helix	182-194	13
β-strand	199-201	3	22
β-strand	209	1	23
β-strand	212	1	23
α-helix	214-232	19
β-strand	237-239	3	22
β-strand	240-241	2	21
α-helix	247-260	14
β-strand	264-268	5	21
α-helix	269-272	4
α-helix	274-287	14
β-strand	290-294	5	21
α-helix	298-302	5
β-strand	308-309	2	19
α-helix	311-321	11
β-strand	325-327	3	21
β-strand	335	1	24
α-helix	339-350	12
β-strand	353-354	2	25
β-strand	357	1	26
α-helix	358-360	3
β-strand	362	1	26
β-strand	366-367	2	25
α-helix	371-374	4
β-strand	375-379	5	21
α-helix	384-386	3
α-helix	387-394	8
β-strand	399-401	3	21
α-helix	404-407	4
α-helix	413-432	20
α-helix	437-451	15
α-helix	453-462	10

Chain H: 28 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	21-24	4
β-strand	25	1	30
α-helix	29-32	4
β-strand	36-44	9	30
α-helix	45	1
α-helix	50-60	11
α-helix	70-74	5
α-helix	77-80	4
β-strand	83-89	7	30
α-helix	90	1
β-strand	97-103	7	30
α-helix	105-107	3
α-helix	113-120	8
α-helix	124-126	3
β-strand	127	1	31
β-strand	130-139	10	30
α-helix	142-145	4
α-helix	155-162	8
β-strand	169-171	3	32
β-strand	173	1	33
α-helix	182-194	13
β-strand	199-201	3	33
β-strand	209	1	34
β-strand	212	1	34
α-helix	214-232	19
β-strand	237-239	3	33
β-strand	240-241	2	32
α-helix	247-259	13
β-strand	264-268	5	32
α-helix	269-272	4
α-helix	274-287	14
β-strand	290-294	5	32
α-helix	298-302	5
β-strand	308-309	2	30
α-helix	311-321	11
β-strand	325-327	3	32
β-strand	335	1	35
α-helix	339-350	12
β-strand	353-354	2	36
β-strand	357	1	37
α-helix	358-360	3
β-strand	362	1	37
β-strand	366-367	2	36
α-helix	371-374	4
β-strand	375-379	5	32
α-helix	384-386	3
α-helix	387-394	8
β-strand	399-401	3	32
α-helix	404-407	4
α-helix	413-432	20
α-helix	437-451	15
α-helix	453-462	10

Chain I: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	38
α-helix	20-22	3
α-helix	23-36	14
β-strand	39-45	7	39
β-strand	52	1	40
β-strand	63	1	40
β-strand	68-70	3	39
α-helix	80-93	14
β-strand	98-105	8	39
β-strand	110-118	9	39
β-strand	133	1	38

Chain K: 28 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	16	1	44
α-helix	21-24	4
β-strand	25	1	45
α-helix	29-32	4
β-strand	36-44	9	45
α-helix	45	1
α-helix	50-60	11
β-strand	68	1	44
α-helix	70-74	5
α-helix	77-80	4
β-strand	83-89	7	45
α-helix	90	1
β-strand	97-103	7	45
α-helix	105-107	3
α-helix	113-121	9
α-helix	124-126	3
β-strand	127	1	24
β-strand	130-139	10	45
α-helix	142-145	4
α-helix	155-162	8
β-strand	169-171	3	46
β-strand	173	1	47
α-helix	182-194	13
β-strand	199-201	3	47
β-strand	209	1	48
β-strand	212	1	48
α-helix	214-232	19
β-strand	237-239	3	47
β-strand	240-241	2	46
α-helix	247-260	14
β-strand	264-268	5	46
α-helix	269-272	4
α-helix	274-287	14
β-strand	290-294	5	46
α-helix	298-302	5
β-strand	308-309	2	45
α-helix	311-321	11
β-strand	325-327	3	46
β-strand	335	1	20
α-helix	339-350	12
β-strand	353-354	2	49
β-strand	357	1	50
α-helix	358-360	3
β-strand	362	1	50
β-strand	366-367	2	49
α-helix	371-373	3
β-strand	375-379	5	46
α-helix	384-386	3
α-helix	387-394	8
β-strand	399-401	3	46
α-helix	404-407	4
α-helix	413-432	20
α-helix	437-451	15
α-helix	453-462	10

Chain M: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3	1
β-strand	4	1	51
α-helix	5	1
α-helix	20-22	3
α-helix	23-35	13
β-strand	39-45	7	52
β-strand	52	1	53
β-strand	63	1	53
β-strand	68-70	3	52
α-helix	80-93	14
β-strand	98-105	8	52
β-strand	110-118	9	52
β-strand	133	1	51

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

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, chloroplastic,Ribulose bisphosphate carboxylase…	C, F, I, J, M, P, T, W	protein	134	Chlamydomonas reinhardtii, Spinacia oleracea	P00873 (AlphaFold model), Q43832 (AlphaFold model)

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

>1UZD_1 Ribulose bisphosphate carboxylase large chain (chains A, B, E, H, K, O, R, V)
MVPQTETKAGAGFKAGVKDYRLTYYTPDYVVRDTDILAAFRMTPQPGVPPEECGAAVAAE
SSTGTWTTVWTDGLTSLDRYKGRCYDIEPVPGEDNQYIAYVAYPIDLFEEGSVTNMFTSI
VGNVFGFKALRALRLEDLRIPPAYVKTFVGPPHGIQVERDKLNKYGRGLLGCTIKPKLGL
SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEAIYKAQAETGEVKGHYL
NATAGTCEEMMKRAVCAKELGVPIIMHDYLTGGFTANTSLAIYCRDNGLLLHIHRAMHAV
IDRQRNHGIHFRVLAKALRMSGGDHLHSGTVVGKLEGEREVTLGFVDLMRDDYVEKDRSR
GIYFTQDWCSMPGVMPVASGGIHVWHMPALVEIFGDDACLQFGGGTLGHPWGNAPGAAAN
RVALEACTQARNEGRDLAREGGDVIRSACKWSPELAAACEVWKEIKFEFDTIDKL

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

>1UZD_2 Ribulose bisphosphate carboxylase small chain 1, chloroplastic,Ribulose bisphosphate carboxylase small chain 2, chloroplastic,Ribulose bisphosphate carboxylase small chain 1, chloroplastic (chains C, F, I, J, M, P, T, W)
MMVWTPVNNKMFETFSYLPPLTDEQIAAQVDYIVANGWIPCLEFATDHGFVYREHHNSPG
YYDGRYWTMWKLPMFGCRDPMQVLREIVACTKAFPDAYVRLVAFDNQKQVQIMGFLVQRP
KTARDFQPANKRSV

Ligands and cofactors

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

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

Primary citation

Chimeric Small Subunits Influence Catalysis without Causing Global Conformational Changes in the Crystal Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase. Karkehabadi, S., Peddi, S.R., Anwaruzzaman, M. et al. Biochemistry (2005) 44:9851. DOI 10.1021/BI050537V · 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…
1UW9 2.05 Å, L290F-A222T chlamydomonas Rubisco mutant
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…

Browse structure collections

About this viewer

MolViewer shows 1UZD 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.