1L9T

CRYSTAL STRUCTURE OF THE I257V VARIANT OF THE COPPER-CONTAINING NITRITE REDUCTASE FROM ALCALIGENES FAECALIS S-6

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0006807	biological_process	obsolete nitrogen compound metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0019333	biological_process	denitrification pathway
A	0042128	biological_process	nitrate assimilation
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0050421	molecular_function	nitrite reductase (NO-forming) activity
B	0005507	molecular_function	copper ion binding
B	0006807	biological_process	obsolete nitrogen compound metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0019333	biological_process	denitrification pathway
B	0042128	biological_process	nitrate assimilation
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0050421	molecular_function	nitrite reductase (NO-forming) activity
C	0005507	molecular_function	copper ion binding
C	0006807	biological_process	obsolete nitrogen compound metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0019333	biological_process	denitrification pathway
C	0042128	biological_process	nitrate assimilation
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
C	0050421	molecular_function	nitrite reductase (NO-forming) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 501

Chain	Residue
A	HIS95
A	CYS136
A	HIS145
A	MET150

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 502

Chain	Residue
A	ASP98
A	HIS100
A	HIS135
B	HIS306
B	NO2504

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NO2 B 504

Chain	Residue
A	ASP98
A	HIS100
A	HIS135
A	CU502
A	HOH5296
B	HIS255
B	VAL257
B	HIS306
B	LEU308
B	HOH5304

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 501

Chain	Residue
B	HIS95
B	CYS136
B	HIS145
B	MET150

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 502

Chain	Residue
B	ASP98
B	HIS100
B	HIS135
C	HIS306
C	NO2604

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NO2 C 604

Chain	Residue
B	ASP98
B	HIS100
B	HIS135
B	CU502
B	HOH6004
C	HIS255
C	VAL257
C	HIS306
C	LEU308

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 501

Chain	Residue
C	HIS95
C	CYS136
C	HIS145
C	MET150

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 502

Chain	Residue
A	HIS306
A	NO2704
C	ASP98
C	HIS100
C	HIS135

---

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NO2 A 704

Chain	Residue
A	HIS255
A	VAL257
A	HIS306
A	LEU308
A	HOH5326
C	ASP98
C	HIS100
C	HIS135
C	CU502
C	HOH5309

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: type 1 copper site => ECO:0000269|PubMed:8172899

Chain	Residue	Details
A	HIS95
B	HIS95
C	HIS95

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: type 2 copper site

Chain	Residue	Details
A	HIS100
A	HIS135
B	HIS100
B	HIS135
C	HIS100
C	HIS135

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: type 1 copper site

Chain	Residue	Details
A	CYS136
A	HIS145
A	MET150
B	CYS136
B	HIS145
B	MET150
C	CYS136
C	HIS145
C	MET150

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: type 2 copper site => ECO:0000269|PubMed:8172899

Chain	Residue	Details
A	HIS306
B	HIS306
C	HIS306

---