1P2E

H61A mutant of flavocytochrome c3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008202	biological_process	steroid metabolic process
A	0009055	molecular_function	electron transfer activity
A	0009061	biological_process	anaerobic respiration
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0019645	biological_process	anaerobic electron transport chain
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 810

Chain	Residue
A	THR506
A	MET507
A	GLY508
A	GLU534
A	THR536
A	HOH812

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM A 801

Chain	Residue
A	CYS17
A	HIS18
A	SER73
A	ALA74
A	HIS75
A	HEM802
A	HOH887
A	HOH1055
A	HOH1158
A	HIS8
A	VAL9
A	CYS14

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM A 802

Chain	Residue
A	LEU4
A	PHE7
A	HIS8
A	GLN12
A	SER16
A	CYS36
A	CYS39
A	HIS40
A	HIS72
A	TYR94
A	HEM801
A	HEM803
A	HOH1185
A	HOH1225

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM A 803

Chain	Residue
A	HIS40
A	GLY41
A	VAL46
A	HIS52
A	ALA57
A	HIS58
A	VAL66
A	ALA67
A	CYS68
A	CYS71
A	HIS72
A	PHE90
A	ASN91
A	MET92
A	HEM802
A	HEM804
A	HOH819
A	HOH953
A	HOH1057

---

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM A 804

Chain	Residue
A	HIS54
A	ASN56
A	ALA59
A	SER60
A	PHE62
A	CYS82
A	SER84
A	CYS85
A	HIS86
A	PHE88
A	LEU167
A	GLN338
A	LYS431
A	LYS434
A	HEM803
A	ACY811
A	HOH858
A	HOH1078
A	HOH1156
A	HOH1196

---

site_id	AC6
Number of Residues	41
Details	BINDING SITE FOR RESIDUE FAD A 805

Chain	Residue
A	GLU534
A	GLY547
A	ASN548
A	ALA549
A	ILE550
A	ILE553
A	FUM806
A	HOH827
A	HOH834
A	HOH841
A	HOH862
A	HOH885
A	HOH1172
A	VAL132
A	GLY133
A	GLY135
A	GLY136
A	ALA137
A	GLU156
A	LYS157
A	GLU158
A	GLY162
A	GLY163
A	ASN164
A	ALA165
A	LEU167
A	ALA168
A	ALA169
A	GLY170
A	GLY171
A	THR276
A	GLY278
A	ALA312
A	THR313
A	GLY314
A	GLN338
A	ASP344
A	MET375
A	HIS504
A	HIS505
A	GLY533

---

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FUM A 806

Chain	Residue
A	GLY170
A	HIS365
A	MET375
A	THR377
A	GLU378
A	ARG402
A	HIS504
A	ARG544
A	GLY546
A	GLY547
A	FAD805

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY A 811

Chain	Residue
A	ALA61
A	HEM804

---

Functional Information from PROSITE/UniProt

site_id	PS00028
Number of Residues	23
Details	ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cvs..ChgtLaevaettkHehynaH

Chain	Residue	Details
A	CYS36-HIS58

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:10978153

Chain	Residue	Details
A	THR377

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: axial binding residue => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39

Chain	Residue	Details
A	HIS8
A	HIS18
A	ASP15
A	ASN33
A	CYS36
A	ALA47
A	THR50
A	ALA61

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: covalent => ECO:0007744|PDB:1E39

Chain	Residue	Details
A	CYS14

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: covalent => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39

Chain	Residue	Details
A	CYS17
A	ASN11
A	LEU43
A	VAL46
A	ALA57
A	SER60

---

site_id	SWS_FT_FI5
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39

Chain	Residue	Details
A	ASP27
A	THR146
A	VAL253
A	THR313
A	THR377
A	SER406
A	PHE480
A	GLY509
A	GLN524
A	VAL525
A	THR49
A	VAL66
A	THR69
A	LYS112
A	VAL131
A	PHE139
A	SER140
A	SER144

---

site_id	SWS_FT_FI6
Number of Residues	7
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P83223

Chain	Residue	Details
A	ALA145
A	GLY340
A	ALA352
A	GLY353
A	ASP479
A	MET519
A	LYS522

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1d4c

Chain	Residue	Details
A	HIS504
A	ARG544
A	HIS365
A	ARG402

---