3REQ

METHYLMALONYL-COA MUTASE, SUBSTRATE-FREE STATE (POOR QUALITY STRUCTURE)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE B12 A 800

Chain	Residue
A	LEU119
A	ALA373
A	GLN454
A	ASP608
A	GLY609
A	HIS610
A	ASP611
A	ARG612
A	GLY613
A	ILE617
A	TYR621
A	VAL206
A	GLY653
A	SER655
A	LEU657
A	GLY685
A	GLY686
A	TYR705
A	THR706
A	PRO707
A	THR709
A	ADN801
A	ARG207
A	GLU247
A	GLY333
A	TRP334
A	GLU370
A	ALA371
A	ILE372

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ADN A 801

Chain	Residue
A	TYR89
A	TYR243
A	GLU247
A	GLY333
A	TRP334
A	B12800

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:10387043, ECO:0007744|PDB:4REQ

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

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site_id	SWS_FT_FI2
Number of Residues	14
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
A	GLY140
A	ARG207
A	ASN208
A	TRP334
A	ALA371
A	LEU374
A	HIS610
A	ARG612

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site_id	SWS_FT_FI3
Number of Residues	1
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

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:9772164

Chain	Residue	Details
A	ALA90

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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

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

Chain	Residue	Details
B	GLN208

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site_id	CSA3
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

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

Chain	Residue	Details
A	TYR621

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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

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