1NPJ

Crystal structure of H145A mutant of nitrite reductase from Alcaligenes faecalis

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	3
Details	BINDING SITE FOR RESIDUE CU A 501

Chain	Residue
A	HIS95
A	CYS136
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
A	HOH503
B	HIS306

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU B 501

Chain	Residue
B	CYS136
B	MET150
B	HIS95

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 502

Chain	Residue
B	HIS100
B	HIS135
B	HOH504
C	HIS306

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU C 501

Chain	Residue
C	HIS95
C	CYS136
C	MET150

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 502

Chain	Residue
A	HIS306
C	HIS100
C	HIS135
C	HOH505

---

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	ALA145
A	MET150
B	CYS136
B	ALA145
B	MET150
C	CYS136
C	ALA145
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

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:8515232

Chain	Residue	Details
A	GLN-2
B	GLN-2
C	GLN-2

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
A	PHE64
A	GLY66

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
B	PHE64
B	GLY66

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
C	PHE64
C	GLY66

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
A	ASP98
A	HIS255

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
B	ASP98
B	HIS255

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
C	ASP98
C	HIS255

---