Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1IR1

Crystal Structure of Spinach Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco) Complexed with CO2, Mg2+ and 2-Carboxyarabinitol-1,5-Bisphosphate

Replaces: 1BUR

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 476

Chain	Residue
A	KCX201
A	ASP203
A	GLU204
A	CAP501

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 476

Chain	Residue
B	KCX201
B	ASP203
B	GLU204
B	CAP501

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 476

Chain	Residue
C	ASP203
C	GLU204
C	CAP501
C	KCX201

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 476

Chain	Residue
D	KCX201
D	ASP203
D	GLU204
D	CAP501

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE CAP A 501

Chain	Residue
A	THR173
A	LYS175
A	LYS177
A	KCX201
A	ASP203
A	GLU204
A	HIS294
A	ARG295
A	HIS327
A	LYS334
A	LEU335
A	SER379
A	GLY380
A	GLY381
A	GLY403
A	GLY404
A	MG476
A	HOH503
A	HOH505
A	HOH508
A	HOH520
A	HOH524
A	HOH558
A	HOH580
A	HOH623
C	GLU60
C	THR65
C	TRP66
C	ASN123

site_id	AC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE CAP B 501

Chain	Residue
B	GLU60
B	THR65
B	TRP66
B	ASN123
B	THR173
B	LYS175
B	LYS177
B	KCX201
B	ASP203
B	GLU204
B	HIS294
B	ARG295
B	HIS327
B	LYS334
B	LEU335
B	SER379
B	GLY380
B	GLY381
B	GLY403
B	GLY404
B	MG476
B	HOH507
B	HOH522
B	HOH547
B	HOH548
B	HOH550
B	HOH602
B	HOH695

site_id	AC7
Number of Residues	29
Details	BINDING SITE FOR RESIDUE CAP C 501

Chain	Residue
C	HOH554
C	HOH575
C	HOH598
A	GLU60
A	THR65
A	TRP66
A	ASN123
C	THR173
C	LYS175
C	LYS177
C	KCX201
C	ASP203
C	GLU204
C	HIS294
C	ARG295
C	HIS327
C	LYS334
C	LEU335
C	SER379
C	GLY380
C	GLY381
C	GLY403
C	GLY404
C	MG476
C	HOH502
C	HOH504
C	HOH548
C	HOH549
C	HOH551

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE CAP D 501

Chain	Residue
D	GLU60
D	THR65
D	TRP66
D	ASN123
D	THR173
D	LYS175
D	LYS177
D	KCX201
D	ASP203
D	GLU204
D	HIS294
D	ARG295
D	HIS327
D	LYS334
D	LEU335
D	SER379
D	GLY380
D	GLY381
D	GLY403
D	GLY404
D	MG476
D	HOH507
D	HOH526
D	HOH551
D	HOH555
D	HOH559
D	HOH585
D	HOH610

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
A	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
A	LYS175
B	LYS175
C	LYS175
D	LYS175

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

Chain	Residue	Details
A	HIS294
B	HIS294
C	HIS294
D	HIS294

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

Chain	Residue	Details
A	LYS334
B	THR65
B	GLU204
B	HIS294
B	HIS327
B	LYS334
C	THR65
C	GLU204
C	HIS294
C	HIS327
C	LYS334
D	THR65
D	GLU204
D	HIS294
D	HIS327
D	LYS334
A	HIS294
A	HIS327
A	THR65
A	GLU204

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
A	ASN123
B	ASN123
C	ASN123
D	ASN123

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
C	SER379
D	THR173
D	LYS177
D	SER379
A	THR173
A	LYS177
A	SER379
B	THR173
B	LYS177
B	SER379
C	THR173
C	LYS177

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
D	KCX201
A	KCX201
B	KCX201
C	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
A	ASP203
B	ASP203
C	ASP203
D	ASP203

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

Chain	Residue	Details
A	ARG295
B	ARG295
C	ARG295
D	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
B	GLY403
B	GLY404
C	GLY381
C	GLY403
C	GLY404
D	GLY381
D	GLY403
D	GLY404
A	GLY404
A	GLY381
A	GLY403
B	GLY381

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

Chain	Residue	Details
C	LYS14
A	LYS14
B	LYS14
D	LYS14

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

Chain	Residue	Details
A	LYS334
B	LYS334
C	LYS334
D	LYS334

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

Chain	Residue	Details
A	PRO3
B	PRO3
C	PRO3
D	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
A	KCX201
B	KCX201
C	KCX201
D	KCX201

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