Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1UPM

ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+.

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 476

Chain	Residue
B	LYS177
B	KCX201
B	ASP203
B	GLU204
B	CAP477

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 476

Chain	Residue
E	CAP477
E	LYS177
E	KCX201
E	ASP203
E	GLU204

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA H 476

Chain	Residue
H	LYS177
H	KCX201
H	ASP203
H	GLU204
H	CAP477

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA K 476

Chain	Residue
K	LYS177
K	KCX201
K	ASP203
K	GLU204
K	CAP477

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA L 476

Chain	Residue
L	LYS177
L	KCX201
L	ASP203
L	GLU204
L	CAP477

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA O 476

Chain	Residue
O	LYS177
O	KCX201
O	ASP203
O	GLU204
O	CAP477

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA R 476

Chain	Residue
R	LYS177
R	KCX201
R	ASP203
R	GLU204
R	CAP477

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA V 476

Chain	Residue
V	LYS177
V	KCX201
V	ASP203
V	GLU204
V	CAP477

site_id	AC9
Number of Residues	26
Details	BINDING SITE FOR RESIDUE CAP B 477

Chain	Residue
B	THR173
B	LYS175
B	LYS177
B	KCX201
B	HIS294
B	ARG295
B	HIS327
B	LYS334
B	LEU335
B	SER379
B	GLY380
B	GLY381
B	GLY403
B	GLY404
B	CA476
B	HOH2119
B	HOH2222
B	HOH2259
B	HOH2260
B	HOH2261
B	HOH2262
B	HOH2263
L	GLU60
L	THR65
L	TRP66
L	ASN123

site_id	BC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE CAP E 477

Chain	Residue
E	THR173
E	LYS175
E	LYS177
E	KCX201
E	GLU204
E	HIS294
E	ARG295
E	HIS327
E	LYS334
E	LEU335
E	SER379
E	GLY380
E	GLY381
E	GLY403
E	GLY404
E	CA476
E	HOH2110
E	HOH2180
E	HOH2226
E	HOH2228
E	HOH2295
E	HOH2296
E	HOH2297
H	GLU60
H	THR65
H	TRP66
H	ASN123

site_id	BC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE CAP H 477

Chain	Residue
H	LYS175
H	LYS177
H	KCX201
H	GLU204
H	HIS294
H	ARG295
H	HIS327
H	LYS334
H	LEU335
H	SER379
H	GLY380
H	GLY381
H	GLY403
H	GLY404
H	CA476
H	HOH2112
H	HOH2168
H	HOH2211
H	HOH2212
H	HOH2221
H	HOH2245
H	HOH2246
E	GLU60
E	THR65
E	TRP66
E	ASN123
E	HOH2040
H	THR173

site_id	BC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE CAP K 477

Chain	Residue
K	THR173
K	LYS175
K	LYS177
K	KCX201
K	HIS294
K	ARG295
K	HIS327
K	LYS334
K	LEU335
K	SER379
K	GLY380
K	GLY381
K	GLY403
K	GLY404
K	CA476
K	HOH2112
K	HOH2170
K	HOH2220
K	HOH2221
K	HOH2276
K	HOH2277
K	HOH2278
O	GLU60
O	THR65
O	TRP66
O	ASN123

site_id	BC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE CAP L 477

Chain	Residue
B	GLU60
B	THR65
B	TRP66
B	ASN123
L	THR173
L	LYS175
L	LYS177
L	KCX201
L	HIS294
L	ARG295
L	HIS327
L	LYS334
L	LEU335
L	SER379
L	GLY380
L	GLY381
L	GLY403
L	GLY404
L	CA476
L	HOH2123
L	HOH2185
L	HOH2188
L	HOH2305
L	HOH2306
L	HOH2307
L	HOH2308

site_id	BC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE CAP O 477

Chain	Residue
K	GLU60
K	THR65
K	TRP66
K	ASN123
O	THR173
O	LYS175
O	LYS177
O	KCX201
O	GLU204
O	HIS294
O	ARG295
O	HIS327
O	LYS334
O	LEU335
O	SER379
O	GLY380
O	GLY381
O	GLY403
O	GLY404
O	CA476
O	HOH2117
O	HOH2220
O	HOH2229
O	HOH2258
O	HOH2259
O	HOH2260
O	HOH2261

site_id	BC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE CAP R 477

Chain	Residue
R	THR173
R	LYS175
R	LYS177
R	KCX201
R	HIS294
R	ARG295
R	HIS327
R	LYS334
R	LEU335
R	SER379
R	GLY380
R	GLY381
R	GLY403
R	GLY404
R	CA476
R	HOH2115
R	HOH2177
R	HOH2179
R	HOH2227
R	HOH2289
R	HOH2290
V	GLU60
V	THR65
V	TRP66
V	ASN123
V	HOH2093

site_id	BC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE CAP V 477

Chain	Residue
R	GLU60
R	THR65
R	TRP66
R	ASN123
R	HOH2044
V	THR173
V	LYS175
V	LYS177
V	KCX201
V	HIS294
V	ARG295
V	HIS327
V	LYS334
V	LEU335
V	SER379
V	GLY380
V	GLY381
V	GLY403
V	GLY404
V	CA476
V	HOH2121
V	HOH2182
V	HOH2235
V	HOH2271
V	HOH2272
V	HOH2273
V	HOH2274

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
B	GLY196-GLU204

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:2118958, ECO:0000269\|PubMed:637859, ECO:0000305\|PubMed:9092835

Chain	Residue	Details
B	LYS175
E	LYS175
H	LYS175
K	LYS175
L	LYS175
O	LYS175
R	LYS175
V	LYS175

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:637859

Chain	Residue	Details
B	HIS294
E	HIS294
H	HIS294
K	HIS294
L	HIS294
O	HIS294
R	HIS294
V	HIS294

site_id	SWS_FT_FI3
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX

Chain	Residue	Details
B	THR65
E	LYS334
H	THR65
H	GLU204
H	HIS294
H	HIS327
H	LYS334
K	THR65
K	GLU204
K	HIS294
K	HIS327
B	GLU204
K	LYS334
L	THR65
L	GLU204
L	HIS294
L	HIS327
L	LYS334
O	THR65
O	GLU204
O	HIS294
O	HIS327
B	HIS294
O	LYS334
R	THR65
R	GLU204
R	HIS294
R	HIS327
R	LYS334
V	THR65
V	GLU204
V	HIS294
V	HIS327
B	HIS327
V	LYS334
B	LYS334
E	THR65
E	GLU204
E	HIS294
E	HIS327

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: in homodimeric partner => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX

Chain	Residue	Details
B	ASN123
E	ASN123
H	ASN123
K	ASN123
L	ASN123
O	ASN123
R	ASN123
V	ASN123

site_id	SWS_FT_FI5
Number of Residues	24
Details	BINDING:

Chain	Residue	Details
B	THR173
K	THR173
K	LYS177
K	SER379
L	THR173
L	LYS177
L	SER379
O	THR173
O	LYS177
O	SER379
R	THR173
B	LYS177
R	LYS177
R	SER379
V	THR173
V	LYS177
V	SER379
B	SER379
E	THR173
E	LYS177
E	SER379
H	THR173
H	LYS177
H	SER379

site_id	SWS_FT_FI6
Number of Residues	8
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
B	KCX201
E	KCX201
H	KCX201
K	KCX201
L	KCX201
O	KCX201
R	KCX201
V	KCX201

site_id	SWS_FT_FI7
Number of Residues	8
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
B	ASP203
E	ASP203
H	ASP203
K	ASP203
L	ASP203
O	ASP203
R	ASP203
V	ASP203

site_id	SWS_FT_FI8
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RXO

Chain	Residue	Details
B	ARG295
E	ARG295
H	ARG295
K	ARG295
L	ARG295
O	ARG295
R	ARG295
V	ARG295

site_id	SWS_FT_FI9
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX, ECO:0007744\|PDB:1RXO

Chain	Residue	Details
B	GLY381
K	GLY381
K	GLY403
K	GLY404
L	GLY381
L	GLY403
L	GLY404
O	GLY381
O	GLY403
O	GLY404
R	GLY381
B	GLY403
R	GLY403
R	GLY404
V	GLY381
V	GLY403
V	GLY404
B	GLY404
E	GLY381
E	GLY403
E	GLY404
H	GLY381
H	GLY403
H	GLY404

site_id	SWS_FT_FI10
Number of Residues	8
Details	SITE: Not N6-methylated => ECO:0000269\|PubMed:2928307

Chain	Residue	Details
B	LYS14
E	LYS14
H	LYS14
K	LYS14
L	LYS14
O	LYS14
R	LYS14
V	LYS14

site_id	SWS_FT_FI11
Number of Residues	8
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:8955130

Chain	Residue	Details
B	LYS334
E	LYS334
H	LYS334
K	LYS334
L	LYS334
O	LYS334
R	LYS334
V	LYS334

site_id	SWS_FT_FI12
Number of Residues	8
Details	MOD_RES: N-acetylproline => ECO:0000269\|PubMed:2928307

Chain	Residue	Details
B	PRO3
E	PRO3
H	PRO3
K	PRO3
L	PRO3
O	PRO3
R	PRO3
V	PRO3

site_id	SWS_FT_FI13
Number of Residues	8
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
B	KCX201
E	KCX201
H	KCX201
K	KCX201
L	KCX201
O	KCX201
R	KCX201
V	KCX201

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
B	LYS175
B	HIS294
B	LYS177
B	ASP203
B	HIS327

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
E	LYS175
E	HIS294
E	LYS177
E	ASP203
E	HIS327

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
H	LYS175
H	HIS294
H	LYS177
H	ASP203
H	HIS327

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
K	LYS175
K	HIS294
K	LYS177
K	ASP203
K	HIS327

site_id	CSA5
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
L	LYS175
L	HIS294
L	LYS177
L	ASP203
L	HIS327

site_id	CSA6
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
O	LYS175
O	HIS294
O	LYS177
O	ASP203
O	HIS327

site_id	CSA7
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
R	LYS175
R	HIS294
R	LYS177
R	ASP203
R	HIS327

site_id	CSA8
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
V	LYS175
V	HIS294
V	LYS177
V	ASP203
V	HIS327

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