4C7Z

Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), activated with sodium dithionite and sodium sulfide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0033727	molecular_function	aldehyde dehydrogenase (FAD-independent) activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 918

Chain	Residue
A	HOH2208
A	HOH2213
A	HOH2378
A	HOH3233
A	HOH3234
A	HOH3235

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 920

Chain	Residue
A	HOH3238
A	HOH3239
A	HOH3240
A	HOH2876
A	HOH3236
A	HOH3237

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES A 1908

Chain	Residue
A	GLN99
A	CYS100
A	GLY101
A	CYS103
A	CYS137
A	ARG138
A	CYS139
A	ILE368

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES A 1909

Chain	Residue
A	GLY39
A	CYS40
A	GLU41
A	GLY43
A	GLN44
A	CYS45
A	GLY46
A	CYS48
A	CYS60

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IPA A 1910

Chain	Residue
A	ALA531
A	TYR535
A	LEU626
A	GLY697
A	PEO1916
A	HOH2870

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT A 1911

Chain	Residue
A	ARG460
A	SER461
A	LEU498
A	ALA531
A	PHE532
A	TYR535
A	GLY536
A	GLN539
A	HOH2845

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1912

Chain	Residue
A	ASP263
A	GLU899
A	GLU903
A	HOH2611
A	HOH2612
A	HOH3241

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1913

Chain	Residue
A	LYS248
A	PRO898
A	GLU899
A	HOH2564

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 1914

Chain	Residue
A	TYR892
A	ARG893
A	HOH2708

---

site_id	BC1
Number of Residues	36
Details	BINDING SITE FOR RESIDUE PCD A 1915

Chain	Residue
A	GLN99
A	CYS139
A	THR420
A	PHE421
A	GLY422
A	ALA531
A	PHE532
A	ARG533
A	TRP650
A	HIS653
A	GLY654
A	GLN655
A	GLY656
A	GLY660
A	SER695
A	GLY696
A	GLY697
A	SER698
A	ARG699
A	GLN700
A	GLN701
A	LEU795
A	SER797
A	CYS799
A	ASN800
A	THR804
A	GLN807
A	ALA864
A	SER865
A	GLY866
A	VAL867
A	GLY868
A	GLU869
A	PEO1916
A	HOH3015
A	HOH3052

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEO A 1916

Chain	Residue
A	ALA531
A	GLY696
A	GLY697
A	GLU869
A	IPA1910
A	PCD1915

---

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CEQGQCGAC

Chain	Residue	Details
A	CYS40-CYS48

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	77
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7502041","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 105

Chain	Residue	Details
A	THR873	covalently attached, hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor

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