Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PPC

Oxidized wild type AfNiR exposed to NO (nitrite bound)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
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	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	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 CU1 A 501

Chain	Residue
A	HIS95
A	CYS136
A	HIS145
A	MET150

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 502

Chain	Residue
A	HIS100
A	HIS135
A	NO2503
B	HIS306

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO2 A 503

Chain	Residue
A	HIS100
A	HIS135
A	CU502
B	HIS255
B	ILE257
B	HIS306
B	LEU308
A	ASP98

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ACT A 1510

Chain	Residue
A	GLY140
A	MET141
A	VAL142
A	PRO143
A	TRP144
A	TYR203
A	VAL207
A	MET210
B	GLU313
B	GLU325

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 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	HIS100
B	HIS135
B	NO2503
B	ACT504
C	HIS306

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NO2 B 503

Chain	Residue
B	ASP98
B	HIS100
B	HIS135
B	CU502
B	ACT504
B	HOH1799
C	ILE257
C	HIS306
C	LEU308

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ACT B 504

Chain	Residue
B	ASP98
B	HIS100
B	HIS135
B	ALA137
B	CU502
B	NO2503
B	HOH1799
C	ILE257
C	HIS306

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT B 1503

Chain	Residue
B	THR228
B	GLY229
B	HIS319

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 1504

Chain	Residue
A	GLU113
A	HOH1545
B	ASP173
B	GLY238
B	GLU239
B	LYS240
B	HOH1587

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 1505

Chain	Residue
B	GLY140
B	MET141
B	VAL142
B	PRO143
B	TRP144
B	MET210
C	GLU313

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT B 1506

Chain	Residue
B	PHE282
B	HOH1515
B	HOH1677
B	HOH1682
C	PHE282
C	HOH1642

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 C 501

Chain	Residue
C	HIS95
C	CYS136
C	HIS145
C	MET150

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 502

Chain	Residue
A	HIS306
C	HIS100
C	HIS135
C	NO2503
C	ACT504

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NO2 C 503

Chain	Residue
A	HIS255
A	ILE257
A	HIS306
A	LEU308
C	ASP98
C	HIS100
C	HIS135
C	CU502
C	ACT504
C	HOH1753

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ACT C 504

Chain	Residue
C	HIS135
C	ALA137
C	CU502
C	NO2503
C	HOH1753
A	ILE257
A	HIS306
C	ASP98
C	HIS100

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT C 1507

Chain	Residue
C	VAL59
C	HIS60
C	TYR184
C	THR206
C	HOH1539
C	HOH1622
C	HOH1629

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT C 1508

Chain	Residue
A	GLU313
C	GLY140
C	MET141
C	VAL142
C	PRO143
C	TRP144
C	MET210

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT C 1509

Chain	Residue
C	THR228
C	GLY229
C	ILE300
C	HIS319
C	LYS321

site_id	CC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TRS A 1501

Chain	Residue
A	THR212
A	LEU213
A	THR214
A	HOH1660
A	HOH1701
A	HOH1708
B	THR212
B	LEU213
B	THR214
C	THR212
C	LEU213
C	THR214

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"description":"type 2 copper site"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {"description":"type 1 copper site"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	164
Details	Domain: {"description":"Plastocyanin-like 2"}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP98
A	HIS255

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

Chain	Residue	Details
B	ASP98
B	HIS255

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

Chain	Residue	Details
C	ASP98
C	HIS255

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)