1E60

OXIDIZED DMSO REDUCTASE EXPOSED TO HEPES - Structure II BUFFER

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016491	molecular_function	oxidoreductase activity
A	0043546	molecular_function	molybdopterin cofactor binding
C	0016491	molecular_function	oxidoreductase activity
C	0043546	molecular_function	molybdopterin cofactor binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 901

Chain	Residue
A	LYS117
A	ARG121
A	ASN124
A	TRP196
A	HOH2683
A	HOH2684
A	HOH2685

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 902

Chain	Residue
A	GLN346
A	HOH2333
A	HOH2686
A	LYS314
A	ARG315

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 901

Chain	Residue
C	LYS117
C	ARG121
C	ASN124
C	TRP196
C	HOH2629
C	HOH2630
C	HOH2631

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 902

Chain	Residue
C	GLU412
C	ASP414
C	ARG419
C	LYS747
C	HOH2339
C	HOH2632

---

site_id	AC5
Number of Residues	37
Details	BINDING SITE FOR RESIDUE PGD A 801

Chain	Residue
A	TYR114
A	GLY115
A	TRP116
A	LYS117
A	SER118
A	CYS125
A	TYR146
A	SER147
A	ARG326
A	GLY432
A	GLY433
A	ASN434
A	HIS438
A	GLN440
A	HIS458
A	ASP459
A	PHE460
A	THR463
A	ALA475
A	ARG481
A	ASP511
A	ALA641
A	HIS643
A	LEU648
A	HIS649
A	SER650
A	GLN651
A	GLU715
A	ASN737
A	GLY754
A	GLN755
A	2MO803
A	HOH2144
A	HOH2570
A	HOH2571
A	HOH2625
A	HOH2680

---

site_id	AC6
Number of Residues	33
Details	BINDING SITE FOR RESIDUE PGD A 802

Chain	Residue
A	TRP116
A	SER147
A	ALA185
A	LYS190
A	THR191
A	GLN193
A	ILE194
A	ILE220
A	ASP221
A	PRO222
A	THR225
A	PRO240
A	GLN241
A	ASP243
A	GLY321
A	TRP322
A	SER323
A	ARG326
A	MET327
A	HIS359
A	SER642
A	HIS643
A	PRO644
A	PHE645
A	ARG647
A	LEU648
A	HIS649
A	GLN755
A	2MO803
A	HOH2195
A	HOH2564
A	HOH2655
A	HOH2681

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 2MO A 803

Chain	Residue
A	SER147
A	PGD801
A	PGD802
A	HOH2682
A	TYR114
A	TRP116
A	ASP145
A	TYR146

---

site_id	AC8
Number of Residues	37
Details	BINDING SITE FOR RESIDUE PGD C 801

Chain	Residue
C	TYR114
C	GLY115
C	TRP116
C	LYS117
C	SER118
C	CYS125
C	TYR146
C	SER147
C	ARG326
C	GLY432
C	GLY433
C	ASN434
C	HIS438
C	GLN440
C	HIS458
C	ASP459
C	PHE460
C	THR463
C	ALA475
C	ARG481
C	ASP511
C	ALA641
C	HIS643
C	LEU648
C	HIS649
C	SER650
C	GLN651
C	GLU715
C	ASN737
C	GLY754
C	GLN755
C	2MO803
C	HOH2126
C	HOH2516
C	HOH2569
C	HOH2625
C	HOH2626

---

site_id	AC9
Number of Residues	35
Details	BINDING SITE FOR RESIDUE PGD C 802

Chain	Residue
C	TRP116
C	SER147
C	ALA185
C	ASP187
C	LYS190
C	THR191
C	GLN193
C	ILE194
C	ILE220
C	ASP221
C	PRO222
C	VAL223
C	THR225
C	PRO240
C	GLN241
C	ASP243
C	GLY321
C	TRP322
C	SER323
C	ARG326
C	MET327
C	HIS359
C	SER642
C	HIS643
C	PRO644
C	PHE645
C	ARG647
C	LEU648
C	HIS649
C	GLN755
C	2MO803
C	HOH2183
C	HOH2184
C	HOH2510
C	HOH2627

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 2MO C 803

Chain	Residue
C	TYR114
C	TRP116
C	ASP145
C	TYR146
C	SER147
C	PGD801
C	PGD802

---

Functional Information from PROSITE/UniProt

site_id	PS00490
Number of Residues	18
Details	MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TpTArhADIVLPaTTsyE

Chain	Residue	Details
A	THR463-GLU480

---

site_id	PS00932
Number of Residues	28
Details	MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AaarGIaDgDvVrVhNdrGqiltgVkVT

Chain	Residue	Details
A	ALA676-THR703

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10835270","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10985771","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11502174","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8890912","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466935","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1997","firstPage":"690","lastPage":"700","volume":"2","journal":"J. Biol. Inorg. Chem.","title":"Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82-A resolution and the dithionite-reduced enzyme at 2.8-A resolution.","authors":["McAlpine A.S.","McEwan A.G.","Shaw A.L.","Bailey S."]}}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	SER147

---

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

Chain	Residue	Details
C	SER147

---