Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MKV

Structure of Pisum sativum Rubisco with ABA

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	23
Details	BINDING SITE FOR RESIDUE RUB A 501

Chain	Residue
A	LYS175
A	GLY380
A	GLY381
A	GLY403
A	GLY404
A	HOH624
A	HOH637
A	HOH644
A	HOH670
A	HOH671
A	HOH691
A	LYS177
B	THR65
B	TRP66
B	ASN123
B	HOH727
A	ASP203
A	GLU204
A	ARG295
A	HIS327
A	LYS334
A	LEU335
A	SER379

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 502

Chain	Residue
A	PHE364
A	THR365
A	HOH807

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE RUB B 501

Chain	Residue
A	THR65
A	TRP66
A	ASN123
B	LYS175
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	HOH611
B	HOH637
B	HOH648
B	HOH689
B	HOH691
B	HOH700
B	HOH716

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE A8S B 502

Chain	Residue
B	LEU37
B	TYR85
B	GLU86
B	TYR100
B	ARG139
B	LYS356
B	TYR363
B	PHE364
B	THR365
B	HOH682
B	HOH786

site_id	AC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE RUB C 501

Chain	Residue
C	LYS175
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	HOH616
C	HOH654
C	HOH655
C	HOH656
C	HOH657
C	HOH683
D	THR65
D	TRP66
D	ASN123

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 502

Chain	Residue
C	TYR363
C	PHE364
C	THR365
C	HOH666

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE RUB D 501

Chain	Residue
D	GLY403
D	GLY404
D	HOH678
D	HOH735
D	HOH745
D	HOH746
D	HOH747
D	HOH762
C	THR65
C	TRP66
C	ASN123
D	LYS175
D	GLU204
D	HIS294
D	ARG295
D	HIS327
D	LYS334
D	LEU335
D	SER379
D	GLY380
D	GLY381

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 502

Chain	Residue
D	PHE364
D	THR365
D	HOH719
D	HOH780

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	8
Details	ACT_SITE: Proton acceptor => ECO:0000250

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	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:26197050, ECO:0007744\|PDB:4MKV

Chain	Residue	Details
A	LYS175
B	LYS175
B	LYS177
B	ARG295
B	HIS327
B	LYS334
B	SER379
B	GLY381
B	GLY403
B	GLY404
C	LYS175
A	LYS177
C	LYS177
C	ARG295
C	HIS327
C	LYS334
C	SER379
C	GLY381
C	GLY403
C	GLY404
D	LYS175
D	LYS177
A	ARG295
D	ARG295
D	HIS327
D	LYS334
D	SER379
D	GLY381
D	GLY403
D	GLY404
A	HIS327
A	LYS334
A	SER379
A	GLY381
A	GLY403
A	GLY404

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: via carbamate group => ECO:0000250

Chain	Residue	Details
A	LYS201
B	LYS201
C	LYS201
D	LYS201

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASP203
A	GLU204
B	ASP203
B	GLU204
C	ASP203
C	GLU204
D	ASP203
D	GLU204

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000250

Chain	Residue	Details
A	LYS334
B	LYS334
C	LYS334
D	LYS334

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269\|PubMed:16668742

Chain	Residue	Details
A	LYS14
B	LYS14
C	LYS14
D	LYS14

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000250

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)
		EDMap 2fo-fc (MTZ)