Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5REQ

Methylmalonyl-COA MUTASE, Y89F Mutant, substrate complex

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	47
Details	BINDING SITE FOR RESIDUE B12 A 1800

Chain	Residue
A	PHE117
A	GLY333
A	TRP334
A	GLU370
A	ALA371
A	ALA373
A	LEU374
A	GLN454
A	LEU602
A	GLY609
A	HIS610
A	LEU119
A	ASP611
A	ARG612
A	GLY613
A	VAL616
A	ILE617
A	TYR621
A	SER655
A	LEU657
A	GLY659
A	GLY685
A	HIS122
A	GLY686
A	VAL687
A	TYR705
A	THR706
A	THR709
A	SCD1801
A	MCD1802
A	HOH5096
A	HOH5103
A	HOH5108
A	ALA139
A	HOH5144
A	HOH5174
A	HOH5205
A	HOH5280
A	HOH5406
A	HOH5417
A	HOH5443
A	HOH5452
A	VAL206
A	ARG207
A	THR209
A	HIS244
A	GLU247

site_id	AC2
Number of Residues	40
Details	BINDING SITE FOR RESIDUE SCD A 1801

Chain	Residue
A	TYR75
A	THR77
A	MET78
A	ARG82
A	THR85
A	ARG87
A	PHE89
A	SER114
A	SER162
A	SER164
A	THR166
A	THR195
A	GLN197
A	ARG207
A	ASN236
A	TYR243
A	HIS244
A	ARG283
A	SER285
A	PHE287
A	ARG326
A	HIS328
A	GLN330
A	GLN361
A	SER362
A	B121800
A	HOH5005
A	HOH5006
A	HOH5024
A	HOH5033
A	HOH5034
A	HOH5035
A	HOH5066
A	HOH5099
A	HOH5107
A	HOH5119
A	HOH5193
A	HOH5244
A	HOH5490
B	ARG45

site_id	AC3
Number of Residues	39
Details	BINDING SITE FOR RESIDUE MCD A 1802

Chain	Residue
A	ARG207
A	ASN236
A	TYR243
A	HIS244
A	ARG283
A	SER285
A	PHE287
A	THR327
A	HIS328
A	GLN330
A	GLN361
A	SER362
A	B121800
A	HOH5005
A	HOH5006
A	HOH5024
A	HOH5033
A	HOH5034
A	HOH5035
A	HOH5066
A	HOH5099
A	HOH5107
A	HOH5119
A	HOH5193
A	HOH5244
A	HOH5490
B	ARG45
A	TYR75
A	THR77
A	MET78
A	ARG82
A	THR85
A	ARG87
A	PHE89
A	SER114
A	SER164
A	THR166
A	THR195
A	GLN197

site_id	AC4
Number of Residues	51
Details	BINDING SITE FOR RESIDUE B12 C 2800

Chain	Residue
C	PHE117
C	LEU119
C	HIS122
C	ALA139
C	VAL206
C	ARG207
C	THR209
C	TYR243
C	HIS244
C	GLU247
C	GLY333
C	TRP334
C	LEU336
C	GLU370
C	ALA371
C	ALA373
C	LEU374
C	GLN454
C	LEU602
C	ASP608
C	GLY609
C	HIS610
C	ASP611
C	ARG612
C	GLY613
C	ILE617
C	TYR621
C	SER655
C	LEU657
C	ALA658
C	GLY659
C	GLY685
C	GLY686
C	VAL687
C	TYR705
C	THR706
C	THR709
C	SER714
C	SCD2801
C	MCD2802
C	HOH4096
C	HOH4103
C	HOH4108
C	HOH4144
C	HOH4174
C	HOH4205
C	HOH4280
C	HOH4406
C	HOH4417
C	HOH4443
C	HOH4452

site_id	AC5
Number of Residues	40
Details	BINDING SITE FOR RESIDUE SCD C 2801

Chain	Residue
C	TYR75
C	THR77
C	MET78
C	ARG82
C	THR85
C	ARG87
C	PHE89
C	SER114
C	SER164
C	THR166
C	THR195
C	GLN197
C	ARG207
C	ASN236
C	TYR243
C	HIS244
C	ARG283
C	SER285
C	PHE287
C	ARG326
C	HIS328
C	GLN330
C	GLN361
C	SER362
C	B122800
C	HOH4005
C	HOH4006
C	HOH4024
C	HOH4033
C	HOH4034
C	HOH4035
C	HOH4039
C	HOH4066
C	HOH4099
C	HOH4107
C	HOH4119
C	HOH4193
C	HOH4244
C	HOH4490
D	ARG45

site_id	AC6
Number of Residues	39
Details	BINDING SITE FOR RESIDUE MCD C 2802

Chain	Residue
C	TYR75
C	THR77
C	MET78
C	ARG82
C	THR85
C	ARG87
C	PHE89
C	SER114
C	SER164
C	THR166
C	THR195
C	GLN197
C	ARG207
C	ASN236
C	TYR243
C	HIS244
C	ARG283
C	SER285
C	PHE287
C	HIS328
C	GLN330
C	GLN361
C	SER362
C	B122800
C	HOH4005
C	HOH4006
C	HOH4024
C	HOH4033
C	HOH4034
C	HOH4035
C	HOH4039
C	HOH4066
C	HOH4099
C	HOH4107
C	HOH4119
C	HOH4193
C	HOH4244
C	HOH4490
D	ARG45

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 3001

Chain	Residue
B	GLU177
B	VAL216
B	ASP219
B	ARG223

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 3002

Chain	Residue
B	THR98
B	ARG100
B	ALA106
B	TRP107
B	GLY354
B	ALA355
B	GLU356

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 3003

Chain	Residue
D	GLU177
D	VAL216
D	TRP220
D	ARG223

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 3004

Chain	Residue
D	THR98
D	ARG100
D	ALA106
D	TRP107
D	GLY354
D	ALA355

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	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	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	PHE89
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	PHE89
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	PHE89	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	PHE89	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)