Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1REQ

METHYLMALONYL-COA MUTASE

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	0005737	cellular_component	cytoplasm
A	0016853	molecular_function	isomerase activity
A	0016866	molecular_function	intramolecular transferase activity
A	0019678	biological_process	propionate metabolic process, methylmalonyl pathway
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	0005737	cellular_component	cytoplasm
C	0016853	molecular_function	isomerase activity
C	0016866	molecular_function	intramolecular transferase activity
C	0019678	biological_process	propionate metabolic process, methylmalonyl pathway
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	46
Details	BINDING SITE FOR RESIDUE B12 A 800

Chain	Residue
A	TYR89
A	GLY333
A	TRP334
A	LEU336
A	GLU370
A	ALA371
A	ALA373
A	LEU374
A	GLN454
A	LEU602
A	GLY609
A	ALA116
A	HIS610
A	ASP611
A	ARG612
A	GLY613
A	ILE617
A	TYR621
A	SER655
A	LEU657
A	ALA658
A	GLY659
A	PHE117
A	GLY685
A	GLY686
A	TYR705
A	THR706
A	THR709
A	GOL802
A	HOH825
A	HOH886
A	HOH893
A	HOH896
A	LEU119
A	HOH923
A	HOH962
A	HOH985
A	HOH988
A	HOH994
A	HOH1052
A	HOH1075
A	ALA139
A	VAL206
A	ARG207
A	TYR243
A	GLU247

site_id	AC2
Number of Residues	35
Details	BINDING SITE FOR RESIDUE DCA A 801

Chain	Residue
A	TYR75
A	THR77
A	MET78
A	ARG82
A	THR85
A	ARG87
A	SER114
A	SER164
A	THR166
A	THR195
A	ASN236
A	ARG283
A	SER285
A	PHE287
A	ARG326
A	THR327
A	HIS328
A	GLN361
A	SER362
A	HOH808
A	HOH809
A	HOH828
A	HOH837
A	HOH838
A	HOH839
A	HOH843
A	HOH869
A	HOH889
A	HOH895
A	HOH906
A	HOH977
A	HOH984
A	HOH1011
B	VAL42
B	ARG45

site_id	AC3
Number of Residues	46
Details	BINDING SITE FOR RESIDUE B12 C 800

Chain	Residue
C	GLY609
C	HIS610
C	ASP611
C	ARG612
C	GLY613
C	ILE617
C	TYR621
C	GLY653
C	SER655
C	LEU657
C	GLY659
C	GLY685
C	GLY686
C	TYR705
C	THR706
C	THR709
C	GOL802
C	HOH887
C	HOH894
C	HOH897
C	HOH924
C	HOH961
C	HOH984
C	HOH994
C	HOH1055
C	HOH1059
C	HOH1081
C	HOH1141
C	TYR89
C	PHE117
C	LEU119
C	HIS122
C	ALA139
C	VAL206
C	ARG207
C	THR209
C	GLU247
C	GLY333
C	TRP334
C	LEU336
C	GLU370
C	ALA371
C	ALA373
C	LEU374
C	GLN454
C	LEU602

site_id	AC4
Number of Residues	36
Details	BINDING SITE FOR RESIDUE DCA C 801

Chain	Residue
C	TYR75
C	THR77
C	MET78
C	ARG82
C	THR85
C	ARG87
C	SER114
C	SER164
C	THR166
C	THR195
C	ASN236
C	ARG283
C	SER285
C	ARG326
C	THR327
C	HIS328
C	GLN361
C	SER362
C	HOH808
C	HOH809
C	HOH829
C	HOH838
C	HOH839
C	HOH840
C	HOH844
C	HOH871
C	HOH890
C	HOH896
C	HOH907
C	HOH976
C	HOH983
C	HOH1013
C	HOH1221
C	HOH1271
D	ARG45
D	HOH1380

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 802

Chain	Residue
A	TYR89
A	ARG207
A	TYR243
A	GLN330
A	B12800
A	HOH845
A	HOH1138
A	HOH1254

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1

Chain	Residue
B	GLU114
B	ARG169
B	ASN239
B	ASN243
B	TRP328
B	GLN365

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 639

Chain	Residue
B	THR98
B	ARG100
B	ALA106
B	TRP107
B	GLY354
B	ALA355
B	HOH810
B	HOH859

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 803

Chain	Residue
A	GLU42
A	ALA250
A	THR251
A	HOH804
A	HOH805
A	HOH920
A	HOH927
A	HOH980

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 640

Chain	Residue
B	ARG329
B	ASN446
B	ARG449
B	HIS491
B	ASP493
B	HOH873
B	HOH886

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 802

Chain	Residue
C	TYR89
C	ARG207
C	TYR243
C	GLN330
C	B12800
C	HOH846

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1

Chain	Residue
D	GLU114
D	ARG169
D	ASN239
D	ASN243
D	TRP328
D	GLN365

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 803

Chain	Residue
C	ALA41
C	GLU42
C	THR251
C	HOH804
C	HOH805
C	HOH921
C	HOH928
C	HOH1148

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 639

Chain	Residue
D	ASN446
D	ARG449
D	ALA450
D	LEU453
D	HIS491
D	ARG492
D	ASP493
D	HOH1459

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG381-SER406
B	ARG377-SER402

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	262
Details	Domain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387043","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4REQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1REQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4REQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10387043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1REQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4REQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9772164","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 11456766, 8805541, 10387043

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

site_id	CSA2
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 11456766, 8805541, 10387043

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

site_id	MCSA1
Number of Residues	6
Details	M-CSA 62

Chain	Residue	Details
A	TYR89	electrostatic stabiliser, radical stabiliser
A	TYR243	electrostatic stabiliser, radical stabiliser
A	HIS244	electrostatic stabiliser, proton acceptor, proton donor
A	LYS604	electrostatic stabiliser
A	ASP608	electrostatic stabiliser
A	HIS610	metal ligand

site_id	MCSA2
Number of Residues	6
Details	M-CSA 62

Chain	Residue	Details
C	TYR89	electrostatic stabiliser, radical stabiliser
C	TYR243	electrostatic stabiliser, radical stabiliser
C	HIS244	electrostatic stabiliser, proton acceptor, proton donor
C	LYS604	electrostatic stabiliser
C	ASP608	electrostatic stabiliser
C	HIS610	metal ligand

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