1ET5

CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6

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

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

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

Chain	Residue
A	HIS100
A	HIS135
A	HIS306
A	HOH503

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 504

Chain	Residue
A	HOH524
A	HOH524
A	HOH533
A	HOH533
A	HOH533
A	HOH524

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 505

Chain	Residue
A	ASP251
A	ASP251
A	ASP251

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Functional Information from SwissProt/UniProt

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

Chain	Residue	Details
A	HIS95

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

Chain	Residue	Details
A	HIS100
A	HIS135

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: type 1 copper site

Chain	Residue	Details
A	CYS136
A	HIS145
A	MET150

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: type 2 copper site => ECO:0000269|PubMed:8172899

Chain	Residue	Details
A	HIS306

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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

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

Chain	Residue	Details
A	ASN98
A	HIS255

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