Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8ILM

The cryo-EM structure of eight Rubisco large subunits (RbcL), two Arabidopsis thaliana Rubisco accumulation factors 1 (AtRaf1), and seven Arabidopsis thaliana Bundle Sheath Defective 2 (AtBSD2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004497	molecular_function	monooxygenase activity
A	0005515	molecular_function	protein binding
A	0009853	biological_process	photorespiration
A	0015977	biological_process	carbon fixation
A	0015979	biological_process	photosynthesis
A	0016829	molecular_function	lyase activity
A	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
A	0019253	biological_process	reductive pentose-phosphate cycle
A	0031470	cellular_component	carboxysome
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004497	molecular_function	monooxygenase activity
B	0005515	molecular_function	protein binding
B	0009853	biological_process	photorespiration
B	0015977	biological_process	carbon fixation
B	0015979	biological_process	photosynthesis
B	0016829	molecular_function	lyase activity
B	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
B	0019253	biological_process	reductive pentose-phosphate cycle
B	0031470	cellular_component	carboxysome
B	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0004497	molecular_function	monooxygenase activity
F	0005515	molecular_function	protein binding
F	0009853	biological_process	photorespiration
F	0015977	biological_process	carbon fixation
F	0015979	biological_process	photosynthesis
F	0016829	molecular_function	lyase activity
F	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
F	0019253	biological_process	reductive pentose-phosphate cycle
F	0031470	cellular_component	carboxysome
F	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0004497	molecular_function	monooxygenase activity
G	0005515	molecular_function	protein binding
G	0009853	biological_process	photorespiration
G	0015977	biological_process	carbon fixation
G	0015979	biological_process	photosynthesis
G	0016829	molecular_function	lyase activity
G	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
G	0019253	biological_process	reductive pentose-phosphate cycle
G	0031470	cellular_component	carboxysome
G	0046872	molecular_function	metal ion binding
H	0000287	molecular_function	magnesium ion binding
H	0004497	molecular_function	monooxygenase activity
H	0005515	molecular_function	protein binding
H	0009853	biological_process	photorespiration
H	0015977	biological_process	carbon fixation
H	0015979	biological_process	photosynthesis
H	0016829	molecular_function	lyase activity
H	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
H	0019253	biological_process	reductive pentose-phosphate cycle
H	0031470	cellular_component	carboxysome
H	0046872	molecular_function	metal ion binding
I	0000287	molecular_function	magnesium ion binding
I	0004497	molecular_function	monooxygenase activity
I	0005515	molecular_function	protein binding
I	0009853	biological_process	photorespiration
I	0015977	biological_process	carbon fixation
I	0015979	biological_process	photosynthesis
I	0016829	molecular_function	lyase activity
I	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
I	0019253	biological_process	reductive pentose-phosphate cycle
I	0031470	cellular_component	carboxysome
I	0046872	molecular_function	metal ion binding
J	0000287	molecular_function	magnesium ion binding
J	0004497	molecular_function	monooxygenase activity
J	0005515	molecular_function	protein binding
J	0009853	biological_process	photorespiration
J	0015977	biological_process	carbon fixation
J	0015979	biological_process	photosynthesis
J	0016829	molecular_function	lyase activity
J	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
J	0019253	biological_process	reductive pentose-phosphate cycle
J	0031470	cellular_component	carboxysome
J	0046872	molecular_function	metal ion binding
K	0000287	molecular_function	magnesium ion binding
K	0004497	molecular_function	monooxygenase activity
K	0005515	molecular_function	protein binding
K	0009853	biological_process	photorespiration
K	0015977	biological_process	carbon fixation
K	0015979	biological_process	photosynthesis
K	0016829	molecular_function	lyase activity
K	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
K	0019253	biological_process	reductive pentose-phosphate cycle
K	0031470	cellular_component	carboxysome
K	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LTGISSIEQNRLIVGA

Chain	Residue	Details
D	LEU61-ALA76

site_id	PS00157
Number of Residues	9
Details	RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE

Chain	Residue	Details
A	GLY193-GLU201

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	497
Details	ZN_FING: CR-type => ECO:0000255\|PROSITE-ProRule:PRU00546

Chain	Residue	Details
C	PRO6-THR77
L	PRO6-THR77
M	PRO6-THR77
N	PRO6-THR77
O	PRO6-THR77
P	PRO6-THR77
Q	PRO6-THR77
G	HIS291
H	LYS172
H	HIS291
I	LYS172
I	HIS291
J	LYS172
J	HIS291
K	LYS172
K	HIS291

site_id	SWS_FT_FI2
Number of Residues	56
Details	BINDING: BINDING => ECO:0000269\|PubMed:29217567, ECO:0007744\|PDB:6EKB, ECO:0007744\|PDB:6EKC

Chain	Residue	Details
C	CYS16
C	CYS19
C	CYS27
C	CYS30
C	CYS51
C	CYS54
C	CYS62
C	CYS65
L	CYS16
L	CYS19
L	CYS27
L	CYS30
L	CYS51
L	CYS54
L	CYS62
L	CYS65
M	CYS16
M	CYS19
M	CYS27
M	CYS30
M	CYS51
M	CYS54
M	CYS62
M	CYS65
N	CYS16
N	CYS19
N	CYS27
N	CYS30
N	CYS51
N	CYS54
N	CYS62
N	CYS65
O	CYS16
O	CYS19
O	CYS27
O	CYS30
O	CYS51
O	CYS54
O	CYS62
O	CYS65
P	CYS16
P	CYS19
P	CYS27
P	CYS30
P	CYS51
P	CYS54
P	CYS62
P	CYS65
Q	CYS16
Q	CYS19
Q	CYS27
Q	CYS30
Q	CYS51
Q	CYS54
Q	CYS62
Q	CYS65

site_id	SWS_FT_FI3
Number of Residues	21
Details	BINDING: BINDING => ECO:0000269\|PubMed:29217567, ECO:0007744\|PDB:6EKB

Chain	Residue	Details
C	GLU22
C	CYS24
C	GLU59
L	GLU22
L	CYS24
L	GLU59
M	GLU22
M	CYS24
M	GLU59
N	GLU22
N	CYS24
N	GLU59
O	GLU22
O	CYS24
O	GLU59
P	GLU22
P	CYS24
P	GLU59
Q	GLU22
Q	CYS24
Q	GLU59
H	LYS174
H	ARG292
H	HIS324
H	SER376
I	THR170
I	LYS174
I	ARG292
I	HIS324
I	SER376
J	THR170
J	LYS174
J	ARG292
J	HIS324
J	SER376
K	THR170
K	LYS174
K	ARG292
K	HIS324
K	SER376

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: via carbamate group => ECO:0000269\|PubMed:8245022

Chain	Residue	Details
A	LYS198
B	LYS198
F	LYS198
G	LYS198
H	LYS198
I	LYS198
J	LYS198
K	LYS198

site_id	SWS_FT_FI5
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:8245022

Chain	Residue	Details
A	ASP200
A	GLU201
B	ASP200
B	GLU201
F	ASP200
F	GLU201
G	ASP200
G	GLU201
H	ASP200
H	GLU201
I	ASP200
I	GLU201
J	ASP200
J	GLU201
K	ASP200
K	GLU201

site_id	SWS_FT_FI6
Number of Residues	8
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	LYS331
B	LYS331
F	LYS331
G	LYS331
H	LYS331
I	LYS331
J	LYS331
K	LYS331

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:16593333

Chain	Residue	Details
A	LYS198
B	LYS198
F	LYS198
G	LYS198
H	LYS198
I	LYS198
J	LYS198
K	LYS198

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
A	LYS172	electrostatic stabiliser, metal ligand, proton donor
A	LYS198	metal ligand, nucleophile, proton donor
A	ASP200	metal ligand
A	GLU201	metal ligand
A	HIS291	proton acceptor
A	LYS331	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
B	LYS172	electrostatic stabiliser, metal ligand, proton donor
B	LYS198	metal ligand, nucleophile, proton donor
B	ASP200	metal ligand
B	GLU201	metal ligand
B	HIS291	proton acceptor
B	LYS331	electrostatic stabiliser

site_id	MCSA3
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
F	LYS172	electrostatic stabiliser, metal ligand, proton donor
F	LYS198	metal ligand, nucleophile, proton donor
F	ASP200	metal ligand
F	GLU201	metal ligand
F	HIS291	proton acceptor
F	LYS331	electrostatic stabiliser

site_id	MCSA4
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
G	LYS172	electrostatic stabiliser, metal ligand, proton donor
G	LYS198	metal ligand, nucleophile, proton donor
G	ASP200	metal ligand
G	GLU201	metal ligand
G	HIS291	proton acceptor
G	LYS331	electrostatic stabiliser

site_id	MCSA5
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
H	LYS172	electrostatic stabiliser, metal ligand, proton donor
H	LYS198	metal ligand, nucleophile, proton donor
H	ASP200	metal ligand
H	GLU201	metal ligand
H	HIS291	proton acceptor
H	LYS331	electrostatic stabiliser

site_id	MCSA6
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
I	LYS172	electrostatic stabiliser, metal ligand, proton donor
I	LYS198	metal ligand, nucleophile, proton donor
I	ASP200	metal ligand
I	GLU201	metal ligand
I	HIS291	proton acceptor
I	LYS331	electrostatic stabiliser

site_id	MCSA7
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
J	LYS172	electrostatic stabiliser, metal ligand, proton donor
J	LYS198	metal ligand, nucleophile, proton donor
J	ASP200	metal ligand
J	GLU201	metal ligand
J	HIS291	proton acceptor
J	LYS331	electrostatic stabiliser

site_id	MCSA8
Number of Residues	6
Details	M-CSA 907

Chain	Residue	Details
K	LYS172	electrostatic stabiliser, metal ligand, proton donor
K	LYS198	metal ligand, nucleophile, proton donor
K	ASP200	metal ligand
K	GLU201	metal ligand
K	HIS291	proton acceptor
K	LYS331	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)