1HZU

DOMAIN SWING UPON HIS TO ALA MUTATION IN NITRITE REDUCTASE OF PSEUDOMONAS AERUGINOSA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0050418	molecular_function	hydroxylamine reductase activity
A	0050421	molecular_function	nitrite reductase (NO-forming) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEC A 601

Chain	Residue
A	ARG46
A	LEU79
A	THR84
A	LEU86
A	MET88
A	PRO89
A	HOH758
A	HOH898
A	HOH920
A	CYS47
A	CYS50
A	HIS51
A	GLY60
A	LYS61
A	LEU63
A	ARG71
A	TYR75

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site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE DHE A 602

Chain	Residue
A	THR59
A	ARG156
A	HIS182
A	ILE183
A	ARG185
A	ARG225
A	VAL227
A	ALA283
A	ILE285
A	ASP328
A	ARG372
A	PHE425
A	GLN483
A	THR530
A	PHE533
A	HOH711
A	HOH719
A	HOH850
A	HOH876

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR

Chain	Residue	Details
A	CYS47
A	CYS50

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR

Chain	Residue	Details
A	HIS51
A	MET88

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR

Chain	Residue	Details
A	ARG71
A	THR84
A	ARG225
A	SER226
A	TYR245
A	ARG372
A	GLN483

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: proximal binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR

Chain	Residue	Details
A	HIS182

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 903

Chain	Residue	Details
A	CYS47	covalently attached
A	CYS50	covalently attached
A	HIS51	metal ligand
A	MET88	metal ligand
A	ALA327	electrostatic stabiliser
A	HIS369	electrostatic stabiliser

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