Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8QJ0

Room-temperature Serial Synchrotron Crystallography structure of Spinacia oleracea RuBisCO

Functional Information from GO Data

Chain	GOid	namespace	contents
L	0000287	molecular_function	magnesium ion binding
L	0004497	molecular_function	monooxygenase activity
L	0009507	cellular_component	chloroplast
L	0009853	biological_process	photorespiration
L	0015977	biological_process	carbon fixation
L	0015979	biological_process	photosynthesis
L	0016829	molecular_function	lyase activity
L	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
L	0019253	biological_process	reductive pentose-phosphate cycle
L	0046872	molecular_function	metal ion binding
M	0000287	molecular_function	magnesium ion binding
M	0004497	molecular_function	monooxygenase activity
M	0009507	cellular_component	chloroplast
M	0009853	biological_process	photorespiration
M	0015977	biological_process	carbon fixation
M	0015979	biological_process	photosynthesis
M	0016829	molecular_function	lyase activity
M	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
M	0019253	biological_process	reductive pentose-phosphate cycle
M	0046872	molecular_function	metal ion binding
N	0000287	molecular_function	magnesium ion binding
N	0004497	molecular_function	monooxygenase activity
N	0009507	cellular_component	chloroplast
N	0009853	biological_process	photorespiration
N	0015977	biological_process	carbon fixation
N	0015979	biological_process	photosynthesis
N	0016829	molecular_function	lyase activity
N	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
N	0019253	biological_process	reductive pentose-phosphate cycle
N	0046872	molecular_function	metal ion binding
O	0000287	molecular_function	magnesium ion binding
O	0004497	molecular_function	monooxygenase activity
O	0009507	cellular_component	chloroplast
O	0009853	biological_process	photorespiration
O	0015977	biological_process	carbon fixation
O	0015979	biological_process	photosynthesis
O	0016829	molecular_function	lyase activity
O	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
O	0019253	biological_process	reductive pentose-phosphate cycle
O	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
L	GLY196-GLU204

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:2118958, ECO:0000269\|PubMed:637859, ECO:0000305\|PubMed:9092835

Chain	Residue	Details
L	LYS175
M	LYS175
N	LYS175
O	LYS175

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:637859

Chain	Residue	Details
L	HIS294
M	HIS294
N	HIS294
O	HIS294

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX

Chain	Residue	Details
L	THR65
M	LYS334
N	THR65
N	GLU204
N	HIS294
N	HIS327
N	LYS334
O	THR65
O	GLU204
O	HIS294
O	HIS327
L	GLU204
O	LYS334
L	HIS294
L	HIS327
L	LYS334
M	THR65
M	GLU204
M	HIS294
M	HIS327

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: in homodimeric partner => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX

Chain	Residue	Details
L	ASN123
M	ASN123
N	ASN123
O	ASN123

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
L	THR173
O	THR173
O	LYS177
O	SER379
L	LYS177
L	SER379
M	THR173
M	LYS177
M	SER379
N	THR173
N	LYS177
N	SER379

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: via carbamate group => ECO:0000269\|PubMed:8648644, ECO:0000269\|PubMed:9092835, ECO:0000305\|PubMed:14596800, ECO:0000305\|PubMed:2118958, ECO:0000305\|PubMed:9034362

Chain	Residue	Details
L	KCX201
M	KCX201
N	KCX201
O	KCX201

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8648644, ECO:0000269\|PubMed:9092835, ECO:0000305\|PubMed:14596800, ECO:0000305\|PubMed:2118958, ECO:0000305\|PubMed:9034362

Chain	Residue	Details
L	ASP203
M	ASP203
N	ASP203
O	ASP203

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RXO

Chain	Residue	Details
L	ARG295
M	ARG295
N	ARG295
O	ARG295

site_id	SWS_FT_FI9
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX, ECO:0007744\|PDB:1RXO

Chain	Residue	Details
L	GLY381
O	GLY381
O	GLY403
O	GLY404
L	GLY403
L	GLY404
M	GLY381
M	GLY403
M	GLY404
N	GLY381
N	GLY403
N	GLY404

site_id	SWS_FT_FI10
Number of Residues	4
Details	SITE: Not N6-methylated => ECO:0000269\|PubMed:2928307

Chain	Residue	Details
L	LYS14
M	LYS14
N	LYS14
O	LYS14

site_id	SWS_FT_FI11
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:8955130

Chain	Residue	Details
L	LYS334
M	LYS334
N	LYS334
O	LYS334

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: N-acetylproline => ECO:0000269\|PubMed:2928307

Chain	Residue	Details
L	PRO3
M	PRO3
N	PRO3
O	PRO3

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:14596800, ECO:0000269\|PubMed:2118958, ECO:0000269\|PubMed:8648644, ECO:0000269\|PubMed:9034362, ECO:0000269\|PubMed:9092835

Chain	Residue	Details
L	KCX201
M	KCX201
N	KCX201
O	KCX201

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)