1NIB

THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0006807	biological_process	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	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	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	TYPE I CU (A 501) BINDING SITE IN CHAIN A

Chain	Residue
A	HIS95
A	CYS136
A	HIS145
A	MET150

---

site_id	AC2
Number of Residues	3
Details	TYPE II CU (A 502) BINDING SITE IN CHAIN A

Chain	Residue
A	HIS100
A	HIS135
A	HOH503

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 501

Chain	Residue
A	HIS95
A	CYS136
A	HIS145
A	MET150

---

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

Chain	Residue
A	HIS100
A	HIS135
A	HOH503
B	HIS306

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 501

Chain	Residue
B	HIS95
B	CYS136
B	HIS145
B	MET150

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 502

Chain	Residue
B	ASP98
B	HIS100
B	HIS135
B	HOH503
C	HIS306

---

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	HIS255
A	HIS306
A	HOH504
C	HIS100
C	HIS135

---

site_id	BC1
Number of Residues	4
Details	TYPE I CU (B 501) BINDING SITE IN CHAIN B

Chain	Residue
B	HIS145
B	MET150
B	HIS95
B	CYS136

---

site_id	BC2
Number of Residues	3
Details	TYPE II CU (B 502) BINDING SITE IN CHAIN B

Chain	Residue
B	HIS100
B	HIS135
B	HOH503

---

site_id	CC1
Number of Residues	4
Details	TYPE I CU (C 501) BINDING SITE IN CHAIN C

Chain	Residue
C	HIS95
C	CYS136
C	HIS145
C	MET150

---

site_id	CC2
Number of Residues	3
Details	TYPE II CU (C 502) BINDING SITE IN CHAIN C

Chain	Residue
C	HIS100
C	HIS135
A	HOH504

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: type 1 copper site

Chain	Residue	Details
A	HIS95
A	CYS136
C	MET150
A	HIS145
A	MET150
B	HIS95
B	CYS136
B	HIS145
B	MET150
C	HIS95
C	CYS136
C	HIS145

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: type 2 copper site

Chain	Residue	Details
A	HIS100
A	HIS135
C	HIS306
A	HIS306
B	HIS100
B	HIS135
B	HIS306
C	HIS100
C	HIS135

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	11
Details	M-CSA 4

Chain	Residue	Details
A	HIS95	metal ligand
A	ASP98	activator, hydrogen bond acceptor, proton acceptor, proton donor
A	HIS100	metal ligand
A	HIS135	metal ligand, single electron acceptor, single electron donor, single electron relay
A	CYS136	metal ligand, single electron acceptor, single electron donor, single electron relay
A	HIS145	metal ligand
A	MET150	metal ligand
A	HIS255	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU279	electrostatic stabiliser, modifies pKa
A	THR280	electrostatic stabiliser, modifies pKa
A	HIS306	metal ligand

---

site_id	MCSA2
Number of Residues	11
Details	M-CSA 4

Chain	Residue	Details
B	HIS95	metal ligand
B	ASP98	activator, hydrogen bond acceptor, proton acceptor, proton donor
B	HIS100	metal ligand
B	HIS135	metal ligand, single electron acceptor, single electron donor, single electron relay
B	CYS136	metal ligand, single electron acceptor, single electron donor, single electron relay
B	HIS145	metal ligand
B	MET150	metal ligand
B	HIS255	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU279	electrostatic stabiliser, modifies pKa
B	THR280	electrostatic stabiliser, modifies pKa
B	HIS306	metal ligand

---

site_id	MCSA3
Number of Residues	11
Details	M-CSA 4

Chain	Residue	Details
C	HIS95	metal ligand
C	ASP98	activator, hydrogen bond acceptor, proton acceptor, proton donor
C	HIS100	metal ligand
C	HIS135	metal ligand, single electron acceptor, single electron donor, single electron relay
C	CYS136	metal ligand, single electron acceptor, single electron donor, single electron relay
C	HIS145	metal ligand
C	MET150	metal ligand
C	HIS255	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLU279	electrostatic stabiliser, modifies pKa
C	THR280	electrostatic stabiliser, modifies pKa
C	HIS306	metal ligand

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