Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5D4H

High-resolution nitrite complex of a copper nitrite reductase determined by synchrotron radiation crystallography

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 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
A	NO2503
C	HIS306

site_id	AC3
Number of Residues	9
Details	binding site for residue NO2 A 503

Chain	Residue
A	ASP98
A	HIS100
A	HIS135
A	CU502
A	HOH603
C	HIS255
C	ILE257
C	HIS306
C	LEU308

site_id	AC4
Number of Residues	10
Details	binding site for residue NO2 A 504

Chain	Residue
A	HIS255
A	ILE257
A	HIS306
A	LEU308
A	HOH710
B	ASP98
B	HIS100
B	HIS135
B	CU502
B	HOH606

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL A 505

Chain	Residue
A	ILE52
A	ASP53
A	ASP54
A	VAL224
A	HOH676
A	HOH814

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL A 506

Chain	Residue
A	TYR193
A	THR216
A	HIS217
A	GLU313
A	LEU314
A	HOH722
B	ARG211

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL A 507

Chain	Residue
A	VAL142
A	HOH603
A	HOH644
A	HOH702
C	ALA302
C	HOH796

site_id	AC8
Number of Residues	9
Details	binding site for residue GOL A 508

Chain	Residue
A	LEU213
A	ARG250
A	HOH602
A	HOH621
A	HOH759
C	ARG253
C	ASN307
C	GLU310
C	HOH610

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL A 509

Chain	Residue
A	ASP230
A	LYS231
A	HOH607
A	HOH631
A	HOH686
A	HOH741

site_id	AD1
Number of Residues	8
Details	binding site for residue GOL A 510

Chain	Residue
A	GLY229
A	ASP230
A	ALA232
A	THR234
A	LYS321
A	HOH615
A	HOH620
A	HOH774

site_id	AD2
Number of Residues	5
Details	binding site for residue GOL A 511

Chain	Residue
A	PHE24
A	VAL25
A	LYS174
A	ILE175
A	HOH671

site_id	AD3
Number of Residues	3
Details	binding site for residue GOL A 512

Chain	Residue
A	LYS174
A	THR234
A	HOH617

site_id	AD4
Number of Residues	2
Details	binding site for residue GOL A 513

Chain	Residue
A	GLU46
A	LYS48

site_id	AD5
Number of Residues	3
Details	binding site for residue GOL A 514

Chain	Residue
A	TRP326
A	THR332
A	SER333

site_id	AD6
Number of Residues	1
Details	binding site for residue GOL A 515

Chain	Residue
A	HOH847

site_id	AD7
Number of Residues	6
Details	binding site for residue ACY A 516

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

site_id	AD8
Number of Residues	4
Details	binding site for residue CU B 501

Chain	Residue
B	HIS95
B	CYS136
B	HIS145
B	MET150

site_id	AD9
Number of Residues	6
Details	binding site for residue CU B 502

Chain	Residue
B	HIS135
A	HIS306
A	NO2504
A	HOH710
B	ASP98
B	HIS100

site_id	AE1
Number of Residues	9
Details	binding site for residue NO2 B 503

Chain	Residue
B	HIS255
B	ILE257
B	HIS306
B	HOH706
C	ASP98
C	HIS100
C	HIS135
C	CU502
C	HOH609

site_id	AE2
Number of Residues	6
Details	binding site for residue GOL B 504

Chain	Residue
A	ALA302
B	PRO139
B	VAL142
B	HOH633
B	HOH676
B	HOH748

site_id	AE3
Number of Residues	8
Details	binding site for residue GOL B 505

Chain	Residue
B	VAL59
B	VAL147
B	SER148
B	PHE183
B	TYR184
B	THR206
B	HOH619
B	HOH704

site_id	AE4
Number of Residues	6
Details	binding site for residue GOL B 506

Chain	Residue
B	TRP326
B	THR332
B	SER333
B	HOH625
B	HOH831
B	HOH908

site_id	AE5
Number of Residues	7
Details	binding site for residue GOL B 507

Chain	Residue
B	TYR193
B	THR216
B	HIS217
B	VAL224
B	GLU313
B	LEU314
C	ARG211

site_id	AE6
Number of Residues	7
Details	binding site for residue ACY B 508

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

site_id	AE7
Number of Residues	4
Details	binding site for residue CU C 501

Chain	Residue
C	HIS95
C	CYS136
C	HIS145
C	MET150

site_id	AE8
Number of Residues	6
Details	binding site for residue CU C 502

Chain	Residue
B	HIS306
B	NO2503
B	HOH706
C	ASP98
C	HIS100
C	HIS135

site_id	AE9
Number of Residues	12
Details	binding site for residue GOL C 503

Chain	Residue
A	THR212
A	LEU213
A	THR214
B	THR212
B	LEU213
B	THR214
C	THR212
C	LEU213
C	THR214
C	HOH604
C	HOH606
C	HOH610

site_id	AF1
Number of Residues	5
Details	binding site for residue GOL C 504

Chain	Residue
B	HOH687
C	PRO139
C	VAL142
C	HOH603
C	HOH628

site_id	AF2
Number of Residues	4
Details	binding site for residue GOL C 505

Chain	Residue
C	TRP326
C	THR332
C	SER333
C	GOL509

site_id	AF3
Number of Residues	5
Details	binding site for residue GOL C 506

Chain	Residue
C	ALA27
C	HIS28
C	GLN30
C	HOH607
C	HOH756

site_id	AF4
Number of Residues	9
Details	binding site for residue GOL C 507

Chain	Residue
C	GLN15
C	HIS26
C	HIS28
C	LYS37
C	VAL39
C	VAL74
C	VAL75
C	HOH615
C	HOH767

site_id	AF5
Number of Residues	8
Details	binding site for residue GOL C 508

Chain	Residue
A	ARG211
C	THR216
C	HIS217
C	VAL224
C	GLU313
C	LEU314
C	HOH602
C	HOH665

site_id	AF6
Number of Residues	4
Details	binding site for residue GOL C 509

Chain	Residue
A	ALA105
C	TRP326
C	GOL505
C	HOH622

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	492
Details	Domain: {"description":"Plastocyanin-like 2"}

Chain

Residue

Details

site_id	SWS_FT_FI2
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_FI3
Number of Residues	6
Details	Binding site: {"description":"type 2 copper site"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	9
Details	Binding site: {"description":"type 1 copper site"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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