1E6V

Methyl-coenzyme M reductase from Methanopyrus kandleri

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0015948	biological_process	methanogenesis
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
A	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity
B	0015948	biological_process	methanogenesis
B	0016740	molecular_function	transferase activity
B	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity
C	0015948	biological_process	methanogenesis
C	0016740	molecular_function	transferase activity
C	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity
D	0005737	cellular_component	cytoplasm
D	0015948	biological_process	methanogenesis
D	0016740	molecular_function	transferase activity
D	0046872	molecular_function	metal ion binding
D	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity
E	0015948	biological_process	methanogenesis
E	0016740	molecular_function	transferase activity
E	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity
F	0015948	biological_process	methanogenesis
F	0016740	molecular_function	transferase activity
F	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE F43 A 1553

Chain	Residue
A	ALA147
D	GLY329
D	GLY330
D	VAL331
D	GLY332
D	PHE333
D	THR334
D	GLN335
D	TYR336
D	PHE399
D	GLY400
A	VAL148
D	PHE446
E	SER366
E	ILE367
E	TYR368
F	SER122
F	GLY123
F	ARG124
F	ALA157
F	THR158
F	VAL159
A	VAL149
F	HIS160
F	HIS162
A	GLN150
A	MET153
A	GLN233
A	MET236
A	ALA246
A	COM1555

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TP7 A 1554

Chain	Residue
A	ARG273
A	LEU323
A	MET327
A	SER328
A	PHE446
A	MET483
A	ASN484
A	VAL485
B	TYR368
B	GLY370
B	HIS380
B	VAL382
D	ARG228
D	LYS259
D	HIS260

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE COM A 1555

Chain	Residue
A	F431553
D	TYR336
D	PHE446
D	TYR447
E	PHE362
E	TYR368
F	LEU121
F	ARG124

---

site_id	AC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE F43 D 1553

Chain	Residue
A	GLY329
A	GLY330
A	VAL331
A	GLY332
A	PHE333
A	THR334
A	GLN335
A	TYR336
A	PHE399
A	GLY400
A	PHE446
B	SER366
B	ILE367
B	TYR368
C	SER122
C	GLY123
C	ARG124
C	ALA157
C	THR158
C	VAL159
C	HIS160
C	HIS162
D	ALA147
D	VAL148
D	VAL149
D	GLN150
D	MET153
D	GLN233
D	MET236
D	ALA246
D	COM1555

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TP7 D 1554

Chain	Residue
E	VAL382
A	ARG228
A	LYS259
A	HIS260
D	ARG273
D	LEU323
D	MET327
D	SER328
D	PHE446
D	MET483
D	ASN484
D	VAL485
E	TYR368
E	GLY370
E	HIS380

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE COM D 1555

Chain	Residue
A	TYR336
A	PHE446
A	TYR447
B	PHE362
B	TYR368
C	LEU121
C	ARG124
D	F431553

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269|PubMed:11023796, ECO:0007744|PDB:1E6V

Chain	Residue	Details
A	GLN150
D	GLN150

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:11023796, ECO:0007744|PDB:1E6V

Chain	Residue	Details
A	LYS259
A	ARG273
A	TYR336
A	TYR447
D	LYS259
D	ARG273
D	TYR336
D	TYR447

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP504
A	GLY468
B	TYR368

---

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

Chain	Residue	Details
D	ASP504
D	GLY468
E	TYR368

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