5N1Q

METHYL-COENZYME M REDUCTASE III FROM METHANOTHERMOCOCCUS THERMOLITHOTROPHICUS AT 1.9 A RESOLUTION

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	0005737	cellular_component	cytoplasm
B	0015948	biological_process	methanogenesis
B	0016740	molecular_function	transferase activity
B	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity
C	0005737	cellular_component	cytoplasm
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	0005737	cellular_component	cytoplasm
E	0015948	biological_process	methanogenesis
E	0016740	molecular_function	transferase activity
E	0050524	molecular_function	coenzyme-B sulfoethylthiotransferase activity
F	0005737	cellular_component	cytoplasm
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	20
Details	binding site for residue TP7 A 601

Chain	Residue
A	ARG274
A	HOH781
A	HOH837
B	PHE362
B	TYR367
B	GLY369
B	HIS379
B	VAL380
B	HOH761
D	ARG229
D	LYS260
A	LEU323
D	MHS261
A	MET327
A	PHE333
A	PHE446
A	MET483
A	ASN484
A	VAL485
A	HOH724

---

site_id	AC2
Number of Residues	37
Details	binding site for residue F43 A 602

Chain	Residue
A	ALA148
A	VAL149
A	VAL150
A	GLN151
A	GLN234
A	MET237
A	ALA247
A	COM604
A	HOH735
A	HOH746
A	HOH759
A	HOH815
A	HOH900
A	HOH919
D	GLY329
D	GLY330
D	VAL331
D	GLY332
D	PHE333
D	THR334
D	GLN335
D	TYR336
D	GLY400
D	GLY445
D	PHE446
D	HOH817
E	SER365
E	ILE366
E	TYR367
F	LEU120
F	SER121
F	GLY122
F	ALA157
F	THR158
F	VAL159
F	HIS160
F	HIS162

---

site_id	AC3
Number of Residues	8
Details	binding site for residue K A 603

Chain	Residue
A	ARG106
A	GLY219
A	ARG220
A	CYS222
D	ARG106
D	GLY219
D	ARG220
D	CYS222

---

site_id	AC4
Number of Residues	10
Details	binding site for residue COM A 604

Chain	Residue
A	F43602
A	HOH742
D	TYR336
D	PHE446
D	TYR447
E	PHE361
E	SER365
E	TYR367
F	LEU120
F	ARG123

---

site_id	AC5
Number of Residues	10
Details	binding site for residue GOL B 501

Chain	Residue
B	LEU121
B	GLU122
B	ALA124
B	HOH606
B	HOH680
E	VAL39
E	LYS40
E	LYS43
E	LEU121
E	HOH771

---

site_id	AC6
Number of Residues	9
Details	binding site for residue COM D 601

Chain	Residue
A	TYR336
A	PHE446
A	TYR447
B	PHE361
B	TYR367
C	LEU120
C	ARG123
D	F43602
D	HOH718

---

site_id	AC7
Number of Residues	37
Details	binding site for residue F43 D 602

Chain	Residue
A	THR334
A	GLN335
A	TYR336
A	GLY400
A	GLY445
A	PHE446
B	SER365
B	ILE366
B	TYR367
C	LEU120
C	SER121
C	GLY122
C	ARG123
C	ALA157
C	THR158
C	VAL159
C	HIS160
C	HIS162
D	ALA148
D	VAL149
D	VAL150
D	GLN151
D	GLN234
D	MET237
D	ALA247
D	COM601
D	HOH708
D	HOH721
D	HOH729
D	HOH741
D	HOH820
D	HOH826
A	GLY329
A	GLY330
A	VAL331
A	GLY332
A	PHE333

---

site_id	AC8
Number of Residues	19
Details	binding site for residue TP7 D 603

Chain	Residue
A	ARG229
A	LYS260
A	MHS261
D	ARG274
D	LEU323
D	MET327
D	PHE333
D	PHE446
D	MET483
D	ASN484
D	VAL485
D	HOH747
D	HOH762
D	HOH764
D	HOH765
E	TYR367
E	GLY369
E	HIS379
E	VAL380

---

site_id	AC9
Number of Residues	8
Details	binding site for residue GOL D 604

Chain	Residue
A	LYS39
A	LEU73
A	MET74
A	GLY87
A	ASP88
A	HOH851
D	HIS153
D	MET154

---

site_id	AD1
Number of Residues	6
Details	binding site for residue MG E 501

Chain	Residue
C	HOH428
E	HOH644
E	HOH736
E	HOH818
F	HOH403
F	HOH486

---

site_id	AD2
Number of Residues	5
Details	binding site for residue GOL F 301

Chain	Residue
A	TYR243
A	LYS244
F	HIS45
F	ARG86
F	ARG197

---

site_id	AD3
Number of Residues	17
Details	binding site for Ligand residues MGN A 403 through ARG A 404 bound to SER A 402

Chain	Residue
A	GLN335
A	TYR388
A	LEU395
A	HIS398
A	PHE399
A	GLY400
A	GLY401
A	SER402
A	ALA405
A	ALA406
A	VAL407
A	ALA408
A	HOH791
A	HOH845
C	MET94
C	HIS162
C	SER163

---

site_id	AD4
Number of Residues	17
Details	binding site for Ligand residues MGN D 403 through ARG D 404 bound to SER D 402

Chain	Residue
D	GLN335
D	TYR388
D	LEU395
D	HIS398
D	PHE399
D	GLY400
D	GLY401
D	SER402
D	ALA405
D	ALA406
D	VAL407
D	ALA408
D	HOH810
D	HOH864
F	MET94
F	HIS162
F	SER163

---

site_id	AD5
Number of Residues	12
Details	binding site for Di-peptide LYS D 260 and MHS D 261

Chain	Residue
A	ARG274
A	TP7601
A	HOH733
B	TYR367
D	ALA232
D	SER256
D	TYR257
D	ALA258
D	ALA259
D	ALA262
D	ASP263
D	VAL264

---

site_id	AD6
Number of Residues	7
Details	binding site for Di-peptide MHS D 261 and ALA D 262

Chain	Residue
A	ARG274
A	TP7601
B	LYS65
D	TYR257
D	ALA258
D	LYS260
D	ASP263

---

site_id	AD7
Number of Residues	11
Details	binding site for Di-peptide ARG D 274 and AGM D 275

Chain	Residue
A	ARG229
A	MHS261
D	LEU271
D	PRO272
D	ALA273
D	SER276
D	ARG277
D	ASN477
D	TP7603
D	HOH764
E	GLU186

---

site_id	AD8
Number of Residues	14
Details	binding site for Di-peptide AGM D 275 and SER D 276

Chain	Residue
A	LEU271
A	ARG277
A	GLY278
A	HOH780
D	LEU271
D	PRO272
D	ALA273
D	ARG274
D	ARG277
D	ASN477
D	HOH764
D	HOH896
D	HOH901
E	GLU186

---

site_id	AD9
Number of Residues	14
Details	binding site for Di-peptide TYR D 447 and GL3 D 448

Chain	Residue
A	COM604
A	HOH884
D	PHE446
D	TYR449
D	ASP450
D	LEU451
D	ASN484
D	HOH802
E	VAL357
E	PHE361
E	HIS364
F	GLY118
F	LEU120
F	HOH456

---

site_id	AE1
Number of Residues	14
Details	binding site for Di-peptide GL3 D 448 and TYR D 449

Chain	Residue
D	SER402
D	ALA406
D	GLN434
D	PHE446
D	TYR447
D	ASP450
D	LEU451
D	ASP453
D	ASN484
D	VAL485
D	GLY486
D	HIS487
D	HOH752
E	PHE361

---