Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RUB

A CRYSTAL FORM OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM NICOTIANA TABACUM IN THE ACTIVATED STATE

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	5
Details	BINDING SITE FOR RESIDUE MG A 491

Chain	Residue
A	ASP203
A	GLU204
A	HIS294
A	CAP490
A	FMT492

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 491

Chain	Residue
B	ASP203
B	GLU204
B	HIS294
B	CAP490
B	FMT492

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 491

Chain	Residue
C	ASP203
C	GLU204
C	HIS294
C	CAP490
C	FMT492

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 491

Chain	Residue
D	ASP203
D	GLU204
D	HIS294
D	CAP490
D	FMT492

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CAP A 490

Chain	Residue
A	THR173
A	LYS175
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	MG491
A	FMT492
D	THR65
D	TRP66
D	ASN123

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CAP B 490

Chain	Residue
B	LEU335
B	SER379
B	GLY380
B	GLY381
B	GLY403
B	GLY404
B	MG491
B	FMT492
C	THR65
C	TRP66
C	ASN123
B	THR173
B	LYS175
B	ASP203
B	GLU204
B	HIS294
B	ARG295
B	HIS327
B	LYS334

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CAP C 490

Chain	Residue
B	THR65
B	ASN123
C	THR173
C	LYS175
C	LYS177
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	MG491
C	FMT492

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CAP D 490

Chain	Residue
A	THR65
A	TRP66
A	ASN123
D	THR173
D	LYS175
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	MG491
D	FMT492

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT A 492

Chain	Residue
A	THR173
A	LYS201
A	ASP202
A	ASP203
A	GLU204
A	HIS294
A	HIS327
A	CAP490
A	MG491

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT B 492

Chain	Residue
B	THR173
B	LYS201
B	ASP202
B	ASP203
B	GLU204
B	HIS294
B	HIS327
B	CAP490
B	MG491

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT C 492

Chain	Residue
C	THR173
C	LYS201
C	ASP202
C	ASP203
C	GLU204
C	HIS294
C	HIS327
C	CAP490
C	MG491

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT D 492

Chain	Residue
D	THR173
D	LYS201
D	ASP202
D	ASP203
D	GLU204
D	HIS294
D	HIS327
D	CAP490
D	MG491

site_id	CTA
Number of Residues	13
Details	catalytic site

Chain	Residue
A	LYS175
A	SER379
A	FMT492
A	CAP490
A	MG491
A	LYS177
A	LYS201
A	ASP203
A	GLU204
A	HIS294
A	ARG295
A	HIS298
A	HIS327

site_id	CTB
Number of Residues	13
Details	catalytic site

Chain	Residue
B	LYS175
B	LYS177
B	LYS201
B	ASP203
B	GLU204
B	HIS294
B	ARG295
B	HIS298
B	HIS327
B	SER379
B	FMT492
B	CAP490
B	MG491

site_id	CTC
Number of Residues	13
Details	catalytic site

Chain	Residue
C	LYS175
C	LYS177
C	LYS201
C	ASP203
C	GLU204
C	HIS294
C	ARG295
C	HIS298
C	HIS327
C	SER379
C	FMT492
C	CAP490
C	MG491

site_id	CTD
Number of Residues	13
Details	catalytic site

Chain	Residue
D	LYS175
D	LYS177
D	LYS201
D	ASP203
D	GLU204
D	HIS294
D	ARG295
D	HIS298
D	HIS327
D	SER379
D	FMT492
D	CAP490
D	MG491

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DLSQEQLLSevEY

Chain	Residue	Details
S	ASP20-TYR32

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	8
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	LYS175
A	HIS294
B	LYS175
B	HIS294
C	LYS175
C	HIS294
D	LYS175
D	HIS294

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: in homodimeric partner

Chain	Residue	Details
A	ASN123
B	ASN123
C	ASN123
D	ASN123

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING:

Chain	Residue	Details
A	THR173
B	ASP203
B	GLU204
B	ARG295
B	HIS327
B	SER379
C	THR173
C	LYS177
C	ASP203
C	GLU204
C	ARG295
A	LYS177
C	HIS327
C	SER379
D	THR173
D	LYS177
D	ASP203
D	GLU204
D	ARG295
D	HIS327
D	SER379
A	ASP203
A	GLU204
A	ARG295
A	HIS327
A	SER379
B	THR173
B	LYS177

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: via carbamate group

Chain	Residue	Details
A	LYS201
B	LYS201
C	LYS201
D	LYS201

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	LYS334
B	LYS334
C	LYS334
D	LYS334

site_id	SWS_FT_FI6
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_FI7
Number of Residues	4
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269\|PubMed:2928307

Chain	Residue	Details
A	LYS14
B	LYS14
C	LYS14
D	LYS14

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:10801357

Chain	Residue	Details
A	LYS201
B	LYS201
C	LYS201
D	LYS201

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