1E39

Flavocytochrome C3 from Shewanella frigidimarina histidine 365 mutated to alanine

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
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	HOH2551

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEC A 801

Chain	Residue
A	LEU24
A	SER73
A	ALA74
A	HIS75
A	HOH2025
A	HOH2381
A	HOH2587
A	HOH2588
A	CYS14
A	CYS17
A	HIS18

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEC A 802

Chain	Residue
A	LEU4
A	PHE7
A	HIS8
A	GLN12
A	SER16
A	GLN35
A	CYS36
A	CYS39
A	HIS40
A	TYR94
A	HOH2589

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC A 803

Chain	Residue
A	LEU43
A	HIS52
A	ALA57
A	HIS58
A	VAL66
A	ALA67
A	CYS68
A	CYS71
A	HIS72
A	PHE90
A	ASN91
A	MET92
A	HOH2160
A	HOH2591
A	HOH2592
A	HOH2596

---

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

Chain	Residue
A	HIS54
A	TYR55
A	ASN56
A	SER60
A	HIS61
A	PHE62
A	CYS82
A	SER84
A	CYS85
A	HIS86
A	PHE88
A	LEU167
A	VAL374
A	LYS431
A	LYS434
A	HOH2494
A	HOH2597
A	HOH2598
A	HOH2599
A	HOH2600

---

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

Chain	Residue
A	FUM806
A	HOH2395
A	HOH2568
A	HOH2601
A	HOH2602
A	HOH2603
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	ARG277
A	GLY278
A	ALA312
A	THR313
A	GLY314
A	GLN338
A	ASP344
A	HIS504
A	HIS505
A	GLY533
A	GLU534
A	ARG544
A	GLY547
A	ASN548
A	ALA549
A	ILE550
A	ILE553

---

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

Chain	Residue
A	GLY170
A	MET236
A	MET375
A	THR377
A	GLU378
A	ARG402
A	HIS504
A	ARG544
A	GLY546
A	GLY547
A	FAD805

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 850

Chain	Residue
A	LYS371
A	GLU454
A	HOH2497
A	HOH2604

---

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	ARG402

---

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	HIS40
A	HIS58
A	HIS61
A	HIS72
A	HIS75
A	HIS86

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: covalent => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39

Chain	Residue	Details
A	CYS14
A	CYS17
A	CYS36
A	CYS68
A	CYS71
A	CYS82
A	CYS85

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: covalent => ECO:0007744|PDB:1E39

Chain	Residue	Details
A	CYS39

---

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

Chain	Residue	Details
A	ALA74
A	ALA549
A	ILE550
A	HIS52
A	ASN91
A	TYR94
A	ALA165
A	GLN338
A	ARG402
A	LYS431
A	ALA137
A	GLU156
A	ASN164
A	ALA169
A	GLY171
A	GLY278
A	HIS505
A	GLU534

---

site_id	SWS_FT_FI6
Number of Residues	9
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P83223

Chain	Residue	Details
A	GLY170
A	ASP344
A	TYR361
A	ALA365
A	THR377
A	GLU378
A	HIS504
A	ARG544
A	GLY547

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 20

Chain	Residue	Details
A	ALA365	increase acidity
A	GLU378	proton acceptor, proton donor, proton relay
A	ARG381	proton acceptor, proton donor, proton relay
A	ARG402	proton acceptor, proton donor
A	HIS504	electrostatic stabiliser, proton acceptor, proton donor
A	HIS505	electrostatic stabiliser
A	ARG544	steric role

---