Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4L80

Crystal Structure of Chloroflexus aurantiacus malyl-CoA lyase in complex with magnesium, oxalate, and propionyl-CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0006107	biological_process	oxaloacetate metabolic process
A	0015977	biological_process	carbon fixation
A	0016829	molecular_function	lyase activity
A	0043427	biological_process	carbon fixation by 3-hydroxypropionate cycle
A	0043959	molecular_function	L-erythro-3-methylmalyl-CoA lyase activity
A	0046872	molecular_function	metal ion binding
A	0047777	molecular_function	(S)-citramalyl-CoA lyase activity
A	0050083	molecular_function	malyl-CoA lyase activity
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0006107	biological_process	oxaloacetate metabolic process
B	0015977	biological_process	carbon fixation
B	0016829	molecular_function	lyase activity
B	0043427	biological_process	carbon fixation by 3-hydroxypropionate cycle
B	0043959	molecular_function	L-erythro-3-methylmalyl-CoA lyase activity
B	0046872	molecular_function	metal ion binding
B	0047777	molecular_function	(S)-citramalyl-CoA lyase activity
B	0050083	molecular_function	malyl-CoA lyase activity
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0006107	biological_process	oxaloacetate metabolic process
C	0015977	biological_process	carbon fixation
C	0016829	molecular_function	lyase activity
C	0043427	biological_process	carbon fixation by 3-hydroxypropionate cycle
C	0043959	molecular_function	L-erythro-3-methylmalyl-CoA lyase activity
C	0046872	molecular_function	metal ion binding
C	0047777	molecular_function	(S)-citramalyl-CoA lyase activity
C	0050083	molecular_function	malyl-CoA lyase activity
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0006107	biological_process	oxaloacetate metabolic process
D	0015977	biological_process	carbon fixation
D	0016829	molecular_function	lyase activity
D	0043427	biological_process	carbon fixation by 3-hydroxypropionate cycle
D	0043959	molecular_function	L-erythro-3-methylmalyl-CoA lyase activity
D	0046872	molecular_function	metal ion binding
D	0047777	molecular_function	(S)-citramalyl-CoA lyase activity
D	0050083	molecular_function	malyl-CoA lyase activity
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0006107	biological_process	oxaloacetate metabolic process
E	0015977	biological_process	carbon fixation
E	0016829	molecular_function	lyase activity
E	0043427	biological_process	carbon fixation by 3-hydroxypropionate cycle
E	0043959	molecular_function	L-erythro-3-methylmalyl-CoA lyase activity
E	0046872	molecular_function	metal ion binding
E	0047777	molecular_function	(S)-citramalyl-CoA lyase activity
E	0050083	molecular_function	malyl-CoA lyase activity
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0006107	biological_process	oxaloacetate metabolic process
F	0015977	biological_process	carbon fixation
F	0016829	molecular_function	lyase activity
F	0043427	biological_process	carbon fixation by 3-hydroxypropionate cycle
F	0043959	molecular_function	L-erythro-3-methylmalyl-CoA lyase activity
F	0046872	molecular_function	metal ion binding
F	0047777	molecular_function	(S)-citramalyl-CoA lyase activity
F	0050083	molecular_function	malyl-CoA lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 1VU A 401

Chain	Residue
A	HIS32
A	OXL402
A	HOH579
A	HOH641
A	HOH671
A	HOH712
A	HOH731
A	HOH740
C	MET316
C	ASP318
E	ARG44
A	PHE33
E	1VU401
E	HOH758
A	LYS40
A	ILE41
A	ARG44
A	ASN58
A	ARG92
A	LEU274
A	PRO276

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OXL A 402

Chain	Residue
A	ARG92
A	GLU157
A	GLY181
A	PRO182
A	ALA183
A	ASP184
A	PRO246
A	TRP272
A	1VU401
A	MG403
A	HOH511
A	HOH740
C	ALA320

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 403

Chain	Residue
A	GLU157
A	ASP184
A	OXL402
A	HOH511
A	HOH740

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS A 404

Chain	Residue
A	GLN221
A	ASP222
A	HIS225
B	GLN221
B	ASP222
B	HIS225
C	GLN221
C	ASP222
C	HIS225

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 1VU B 401

Chain	Residue
A	MET316
A	ASP318
A	HOH647
B	HIS32
B	PHE33
B	LYS40
B	ILE41
B	ARG44
B	ALA62
B	ARG92
B	ALA183
B	LEU274
B	PRO276
B	OXL402
B	HOH549
B	HOH597
B	HOH599
B	HOH637
B	HOH745
B	HOH748

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE OXL B 402

Chain	Residue
A	ALA320
B	ARG92
B	LEU155
B	GLU157
B	GLY181
B	PRO182
B	ALA183
B	ASP184
B	PRO246
B	TRP272
B	1VU401
B	MG403
B	HOH606
B	HOH699

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 403

Chain	Residue
B	GLU157
B	ASP184
B	OXL402
B	HOH606
B	HOH699

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 1VU C 401

Chain	Residue
C	HOH503
C	HOH519
C	HOH595
C	HOH625
C	HOH626
C	HOH637
C	HOH663
C	HOH717
F	LYS50
B	MET316
B	ASP318
B	HOH710
C	HIS32
C	PHE33
C	LYS40
C	ILE41
C	ALA62
C	ARG92
C	LEU274
C	PRO276
C	OXL402

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OXL C 402

Chain	Residue
C	ARG92
C	GLU157
C	GLY181
C	PRO182
C	ALA183
C	ASP184
C	PRO246
C	TRP272
C	1VU401
C	MG403
C	HOH502
C	HOH503

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 403

Chain	Residue
C	GLU157
C	ASP184
C	OXL402
C	HOH502
C	HOH503

site_id	BC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE 1VU D 401

Chain	Residue
D	HIS32
D	PHE33
D	LYS40
D	ILE41
D	ARG44
D	ASN58
D	ASP61
D	ALA62
D	ARG92
D	LEU274
D	PRO276
D	OXL402
D	HOH517
D	HOH614
D	HOH660
D	HOH663
D	HOH675
D	HOH687
D	HOH715
D	HOH716
D	HOH728
D	HOH761
D	HOH783
F	MET311
F	MET316
F	ASP318

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OXL D 402

Chain	Residue
D	ARG92
D	LEU155
D	GLU157
D	GLY181
D	PRO182
D	ALA183
D	ASP184
D	PRO246
D	TRP272
D	1VU401
D	MG403
D	HOH502
D	HOH517

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 403

Chain	Residue
D	GLU157
D	ASP184
D	OXL402
D	HOH502
D	HOH517

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS D 404

Chain	Residue
D	GLN221
D	ASP222
D	HIS225
E	GLN221
E	ASP222
E	HIS225
F	GLN221
F	ASP222
F	HIS225

site_id	BC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 1VU E 401

Chain	Residue
A	LYS40
A	1VU401
D	MET311
D	ASP318
E	HIS32
E	PHE33
E	LYS40
E	ILE41
E	ARG44
E	ASN58
E	ASP61
E	ALA62
E	ARG92
E	LYS251
E	LEU274
E	OXL402
E	HOH557
E	HOH605
E	HOH609
E	HOH726
E	HOH779

site_id	BC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OXL E 402

Chain	Residue
D	ALA320
E	ARG92
E	GLU157
E	GLY181
E	PRO182
E	ALA183
E	ASP184
E	PRO246
E	TRP272
E	1VU401
E	MG403
E	HOH609

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 403

Chain	Residue
E	GLU157
E	ASP184
E	OXL402
E	HOH508
E	HOH609

site_id	BC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1VU F 401

Chain	Residue
E	MET316
E	ASP318
F	HIS32
F	PHE33
F	LYS40
F	ILE41
F	ARG44
F	ALA62
F	ARG92
F	ALA183
F	LEU274
F	PRO276
F	OXL402
F	HOH571
F	HOH723

site_id	CC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OXL F 402

Chain	Residue
F	ARG92
F	GLU157
F	GLY181
F	PRO182
F	ALA183
F	ASP184
F	PRO246
F	TRP272
F	1VU401
F	MG403
F	HOH506
F	HOH628

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 403

Chain	Residue
F	GLU157
F	ASP184
F	OXL402
F	HOH506
F	HOH628

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING:

Chain	Residue	Details
C	ARG92
C	ALA183
C	LEU274
D	HIS32
D	LYS40
D	ARG92
D	ALA183
D	LEU274
E	HIS32
E	LYS40
E	ARG92
E	ALA183
E	LEU274
F	HIS32
F	LYS40
F	ARG92
F	ALA183
F	LEU274
A	HIS32
A	LYS40
A	ARG92
A	ALA183
A	LEU274
B	HIS32
B	LYS40
B	ARG92
B	ALA183
B	LEU274
C	HIS32
C	LYS40

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:24206647, ECO:0007744\|PDB:4L80

Chain	Residue	Details
D	GLU157
D	ASP184
E	GLU157
E	ASP184
F	GLU157
F	ASP184
A	GLU157
A	ASP184
B	GLU157
B	ASP184
C	GLU157
C	ASP184

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