3RUB

CRYSTAL STRUCTURE OF THE UNACTIVATED FORM OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM TOBACCO REFINED AT 2.0-ANGSTROMS RESOLUTION

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 L 490

Chain	Residue
L	GLY380
L	GLY381
L	GLY403
L	GLY404
L	HOH608
L	HOH668

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 L 491

Chain	Residue
L	ARG295
L	HIS298
L	GLY329
L	HOH636

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 L 492

Chain	Residue
L	ARG134
L	LYS305
L	HIS310
L	ILE341
L	HOH578

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ASN L 493

Chain	Residue
L	LYS463
L	GLU464
L	PHE467

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site_id	CAT
Number of Residues	13
Details	CATALYTIC RESIDUES

Chain	Residue
L	LYS175
L	SER379
L	SO4490
L	SO4491
L	SO4492
L	LYS177
L	LYS201
L	ASP203
L	GLU204
L	HIS294
L	ARG295
L	HIS298
L	HIS327

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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

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

Chain	Residue	Details
L	GLY196-GLU204

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
L	LYS175
L	HIS294

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: in homodimeric partner

Chain	Residue	Details
L	ASN123

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING:

Chain	Residue	Details
L	THR173
L	LYS177
L	ASP203
L	GLU204
L	ARG295
L	HIS327
L	SER379

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: via carbamate group

Chain	Residue	Details
L	LYS201

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Transition state stabilizer

Chain	Residue	Details
L	LYS334

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N-acetylproline => ECO:0000269|PubMed:2928307

Chain	Residue	Details
L	PRO3

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:2928307

Chain	Residue	Details
L	LYS14

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:10801357

Chain	Residue	Details
L	LYS201

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
L	LYS175
L	LYS201
L	LYS177
L	HIS294
L	ASP203
L	HIS327

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