Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2REQ

METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004494	molecular_function	methylmalonyl-CoA mutase activity
A	0005515	molecular_function	protein binding
A	0016853	molecular_function	isomerase activity
A	0016866	molecular_function	intramolecular transferase activity
A	0031419	molecular_function	cobalamin binding
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004494	molecular_function	methylmalonyl-CoA mutase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0016853	molecular_function	isomerase activity
B	0016866	molecular_function	intramolecular transferase activity
B	0019652	biological_process	lactate fermentation to propionate and acetate
B	0019678	biological_process	propionate metabolic process, methylmalonyl pathway
B	0031419	molecular_function	cobalamin binding
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0004494	molecular_function	methylmalonyl-CoA mutase activity
C	0005515	molecular_function	protein binding
C	0016853	molecular_function	isomerase activity
C	0016866	molecular_function	intramolecular transferase activity
C	0031419	molecular_function	cobalamin binding
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0004494	molecular_function	methylmalonyl-CoA mutase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0016853	molecular_function	isomerase activity
D	0016866	molecular_function	intramolecular transferase activity
D	0019652	biological_process	lactate fermentation to propionate and acetate
D	0019678	biological_process	propionate metabolic process, methylmalonyl pathway
D	0031419	molecular_function	cobalamin binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE COA A 801

Chain	Residue
A	TYR75
A	ARG82
A	LYS321
A	HOH999

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE COA C 801

Chain	Residue
C	TYR75
C	ARG82
C	LYS321
C	HOH994
D	VAL42

site_id	AC3
Number of Residues	36
Details	BINDING SITE FOR RESIDUE B12 A 800

Chain	Residue
A	VAL206
A	ARG207
A	THR209
A	GLU247
A	TRP334
A	GLU370
A	ALA371
A	ALA373
A	GLN454
A	GLY609
A	HIS610
A	ASP611
A	ARG612
A	GLY613
A	ILE617
A	TYR621
A	GLY653
A	SER655
A	LEU657
A	ALA658
A	GLY659
A	GLY685
A	GLY686
A	VAL687
A	TYR705
A	THR706
A	PRO707
A	THR709
A	HOH810
A	HOH848
A	HOH849
A	HOH856
A	HOH857
A	HOH880
A	HOH918
A	HOH1000

site_id	AC4
Number of Residues	39
Details	BINDING SITE FOR RESIDUE B12 C 800

Chain	Residue
C	LEU119
C	VAL206
C	ARG207
C	THR209
C	GLU247
C	TRP334
C	GLU370
C	ALA371
C	ILE372
C	ALA373
C	GLN454
C	LEU602
C	GLY609
C	HIS610
C	ASP611
C	ARG612
C	GLY613
C	ILE617
C	TYR621
C	GLY653
C	SER655
C	LEU657
C	ALA658
C	GLY659
C	GLY685
C	GLY686
C	VAL687
C	TYR705
C	THR706
C	PRO707
C	THR709
C	HOH810
C	HOH847
C	HOH848
C	HOH855
C	HOH856
C	HOH878
C	HOH913
C	HOH995

Functional Information from PROSITE/UniProt

site_id	PS00544
Number of Residues	26
Details	METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTgiVLaEEvnigRvnDPaGGS

Chain	Residue	Details
B	ARG377-SER402
A	ARG381-SER406

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:10387043, ECO:0007744\|PDB:4REQ

Chain	Residue	Details
A	ALA76
A	MET245
A	LEU284
A	PHE286
C	ALA76
C	TYR79
C	PRO83
C	ILE86
C	GLN88
C	ALA90
C	VAL115
A	TYR79
C	ILE196
C	ASN198
C	MET245
C	LEU284
C	PHE286
A	PRO83
A	ILE86
A	GLN88
A	ALA90
A	VAL115
A	ILE196
A	ASN198

site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269\|PubMed:10387043, ECO:0000269\|PubMed:8805541, ECO:0007744\|PDB:1REQ, ECO:0007744\|PDB:4REQ

Chain	Residue	Details
A	ASP118
A	GLY613
A	SER656
A	ALA658
A	VAL687
A	VAL710
C	ASP118
C	GLY140
C	ARG207
C	ASN208
C	TRP334
A	GLY140
C	ALA371
C	LEU374
C	HIS610
C	ARG612
C	GLY613
C	SER656
C	ALA658
C	VAL687
C	VAL710
A	ARG207
A	ASN208
A	TRP334
A	ALA371
A	LEU374
A	HIS610
A	ARG612

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:10387043, ECO:0000269\|PubMed:8805541, ECO:0007744\|PDB:1REQ, ECO:0007744\|PDB:4REQ

Chain	Residue	Details
A	ASP611
C	ASP611

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:9772164

Chain	Residue	Details
A	ALA90
C	ALA90

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1bmt

Chain	Residue	Details
A	ASP608
A	HIS661
A	HIS610

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1bmt

Chain	Residue	Details
C	ASP608
C	HIS661
C	HIS610

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

Chain	Residue	Details
B	GLN208

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

Chain	Residue	Details
D	GLN208

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

Chain	Residue	Details
A	ASP608
A	LYS604
A	TYR89
A	HIS244
A	HIS610

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

Chain	Residue	Details
C	ASP608
C	LYS604
C	TYR89
C	HIS244
C	HIS610

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

Chain	Residue	Details
A	TYR621

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

Chain	Residue	Details
C	TYR621

site_id	MCSA1
Number of Residues	6
Details	M-CSA 62

Chain	Residue	Details
A	ALA90	electrostatic stabiliser, radical stabiliser
A	HIS244	electrostatic stabiliser, radical stabiliser
A	MET245	electrostatic stabiliser, proton acceptor, proton donor
A	MET605	electrostatic stabiliser
A	GLY609	electrostatic stabiliser
A	ASP611	metal ligand

site_id	MCSA2
Number of Residues	6
Details	M-CSA 62

Chain	Residue	Details
C	ALA90	electrostatic stabiliser, radical stabiliser
C	HIS244	electrostatic stabiliser, radical stabiliser
C	MET245	electrostatic stabiliser, proton acceptor, proton donor
C	MET605	electrostatic stabiliser
C	GLY609	electrostatic stabiliser
C	ASP611	metal ligand

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