1N1Q

Crystal structure of a Dps protein from Bacillus brevis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0005737	cellular_component	cytoplasm
A	0006879	biological_process	intracellular iron ion homeostasis
A	0008199	molecular_function	ferric iron binding
A	0009295	cellular_component	nucleoid
A	0016491	molecular_function	oxidoreductase activity
A	0016722	molecular_function	oxidoreductase activity, acting on metal ions
A	0030261	biological_process	chromosome condensation
A	0046872	molecular_function	metal ion binding
B	0003677	molecular_function	DNA binding
B	0005737	cellular_component	cytoplasm
B	0006879	biological_process	intracellular iron ion homeostasis
B	0008199	molecular_function	ferric iron binding
B	0009295	cellular_component	nucleoid
B	0016491	molecular_function	oxidoreductase activity
B	0016722	molecular_function	oxidoreductase activity, acting on metal ions
B	0030261	biological_process	chromosome condensation
B	0046872	molecular_function	metal ion binding
C	0003677	molecular_function	DNA binding
C	0005737	cellular_component	cytoplasm
C	0006879	biological_process	intracellular iron ion homeostasis
C	0008199	molecular_function	ferric iron binding
C	0009295	cellular_component	nucleoid
C	0016491	molecular_function	oxidoreductase activity
C	0016722	molecular_function	oxidoreductase activity, acting on metal ions
C	0030261	biological_process	chromosome condensation
C	0046872	molecular_function	metal ion binding
D	0003677	molecular_function	DNA binding
D	0005737	cellular_component	cytoplasm
D	0006879	biological_process	intracellular iron ion homeostasis
D	0008199	molecular_function	ferric iron binding
D	0009295	cellular_component	nucleoid
D	0016491	molecular_function	oxidoreductase activity
D	0016722	molecular_function	oxidoreductase activity, acting on metal ions
D	0030261	biological_process	chromosome condensation
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FEO B 515

Chain	Residue
A	HIS31
A	HIS43
A	HOH640
A	HOH641
B	ASP58
B	GLU62

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FEO A 516

Chain	Residue
B	HIS31
B	HOH611
B	HOH612
A	ASP58
A	GLU62
A	LYS139

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FEO D 517

Chain	Residue
C	HIS31
C	LYS139
C	HOH657
C	HOH658
D	ASP58
D	GLU62

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FEO C 518

Chain	Residue
C	ASP58
C	GLU62
D	HIS31
D	HOH633
D	HOH634

---

Functional Information from PROSITE/UniProt

site_id	PS00818
Number of Residues	17
Details	DPS_1 Dps protein family signature 1. HWnVnGpnfftLHekfE

Chain	Residue	Details
A	HIS31-GLU47

---

site_id	PS00819
Number of Residues	15
Details	DPS_2 Dps protein family signature 2. IDtLAERvlsIGgsP

Chain	Residue	Details
A	ILE57-PRO71

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12767829

Chain	Residue	Details
A	HIS31
B	HIS31
C	HIS31
D	HIS31

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: in other chain => ECO:0000269|PubMed:12767829

Chain	Residue	Details
A	ASP58
B	ASP58
C	ASP58
D	ASP58

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:12767829

Chain	Residue	Details
A	GLU62
B	GLU62
C	GLU62
D	GLU62

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