Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KYY

Cu(II) complex of HOCl-induced flavoprotein disulfide reductase RclA from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
A	0006979	biological_process	response to oxidative stress
A	0008823	molecular_function	cupric reductase (NADH) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0042803	molecular_function	protein homodimerization activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	1901530	biological_process	response to hypochlorite
B	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
B	0006979	biological_process	response to oxidative stress
B	0008823	molecular_function	cupric reductase (NADH) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
B	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B	0042803	molecular_function	protein homodimerization activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	1901530	biological_process	response to hypochlorite
C	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
C	0006979	biological_process	response to oxidative stress
C	0008823	molecular_function	cupric reductase (NADH) activity
C	0016491	molecular_function	oxidoreductase activity
C	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
C	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
C	0042803	molecular_function	protein homodimerization activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	1901530	biological_process	response to hypochlorite
D	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
D	0006979	biological_process	response to oxidative stress
D	0008823	molecular_function	cupric reductase (NADH) activity
D	0016491	molecular_function	oxidoreductase activity
D	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
D	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
D	0042803	molecular_function	protein homodimerization activity
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	1901530	biological_process	response to hypochlorite

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	binding site for residue FAD A 501

Chain	Residue
A	GLY10
A	THR42
A	CYS43
A	CYS48
A	LYS52
A	GLY97
A	ALA99
A	ASN126
A	THR127
A	GLY128
A	ILE169
A	PHE11
A	ARG252
A	LEU259
A	GLY291
A	ASP292
A	GLN298
A	PHE299
A	THR300
A	TYR301
A	SER303
B	HIS426
A	GLY12
A	LYS13
A	ILE32
A	GLU33
A	GLN34
A	MET38
A	GLY41

site_id	AC2
Number of Residues	1
Details	binding site for residue CU A 502

Chain	Residue
A	HIS61

site_id	AC3
Number of Residues	1
Details	binding site for residue CU A 503

Chain	Residue
A	HIS84

site_id	AC4
Number of Residues	2
Details	binding site for residue CU A 504

Chain	Residue
A	HIS235
A	HIS238

site_id	AC5
Number of Residues	2
Details	binding site for residue CU A 505

Chain	Residue
A	HIS160
A	ALA242

site_id	AC6
Number of Residues	1
Details	binding site for residue CU A 506

Chain	Residue
A	HIS110

site_id	AC7
Number of Residues	1
Details	binding site for residue CU A 507

Chain	Residue
A	HIS119

site_id	AC8
Number of Residues	2
Details	binding site for residue CU A 508

Chain	Residue
A	SER258
A	HIS260

site_id	AC9
Number of Residues	4
Details	binding site for residue CU A 509

Chain	Residue
A	CYS43
A	CYS48
A	THR300
B	HIS426

site_id	AD1
Number of Residues	27
Details	binding site for residue FAD B 501

Chain	Residue
A	HIS426
B	GLY10
B	GLY12
B	LYS13
B	GLU33
B	GLN34
B	MET38
B	THR42
B	CYS43
B	CYS48
B	LYS52
B	GLN98
B	ALA99
B	ASN126
B	THR127
B	GLY128
B	SER148
B	ILE169
B	ARG252
B	GLY291
B	ASP292
B	GLN298
B	PHE299
B	THR300
B	TYR301
B	SER303
B	PHE333

site_id	AD2
Number of Residues	1
Details	binding site for residue CU B 502

Chain	Residue
B	HIS105

site_id	AD3
Number of Residues	1
Details	binding site for residue CU B 503

Chain	Residue
B	HIS260

site_id	AD4
Number of Residues	1
Details	binding site for residue CU B 504

Chain	Residue
B	HIS61

site_id	AD5
Number of Residues	2
Details	binding site for residue CU B 505

Chain	Residue
B	ASN80
B	HIS84

site_id	AD6
Number of Residues	1
Details	binding site for residue CU B 506

Chain	Residue
B	HIS221

site_id	AD7
Number of Residues	2
Details	binding site for residue CU B 507

Chain	Residue
B	HIS238
D	GLU156

site_id	AD8
Number of Residues	1
Details	binding site for residue CU B 508

Chain	Residue
B	HIS235

site_id	AD9
Number of Residues	4
Details	binding site for residue CU B 509

Chain	Residue
A	HIS426
B	CYS43
B	CYS48
B	THR300

site_id	AE1
Number of Residues	1
Details	binding site for residue CL B 510

Chain	Residue
B	ASN327

site_id	AE2
Number of Residues	2
Details	binding site for residue CU C 501

Chain	Residue
B	ARG108
C	ASN327

site_id	AE3
Number of Residues	29
Details	binding site for residue FAD C 502

Chain	Residue
C	LYS52
C	GLN98
C	ALA99
C	ASN126
C	THR127
C	GLY128
C	ILE169
C	ARG252
C	GLY291
C	ASP292
C	GLN298
C	PHE299
C	THR300
C	TYR301
C	SER303
D	HIS426
C	ILE9
C	GLY10
C	GLY12
C	LYS13
C	GLU33
C	GLN34
C	MET38
C	GLY41
C	THR42
C	CYS43
C	ILE46
C	GLY47
C	CYS48

site_id	AE4
Number of Residues	1
Details	binding site for residue CU C 503

Chain	Residue
C	HIS105

site_id	AE5
Number of Residues	1
Details	binding site for residue CU C 504

Chain	Residue
C	HIS227

site_id	AE6
Number of Residues	1
Details	binding site for residue CU C 505

Chain	Residue
C	HIS221

site_id	AE7
Number of Residues	1
Details	binding site for residue CU C 506

Chain	Residue
C	HIS260

site_id	AE8
Number of Residues	1
Details	binding site for residue CU C 507

Chain	Residue
C	HIS61

site_id	AE9
Number of Residues	2
Details	binding site for residue CU C 508

Chain	Residue
C	ASN80
C	HIS84

site_id	AF1
Number of Residues	2
Details	binding site for residue CU C 509

Chain	Residue
B	HIS105
C	GLY352

site_id	AF2
Number of Residues	1
Details	binding site for residue CL C 510

Chain	Residue
C	TYR168

site_id	AF3
Number of Residues	1
Details	binding site for residue CU C 511

Chain	Residue
C	HIS228

site_id	AF4
Number of Residues	29
Details	binding site for residue FAD D 501

Chain	Residue
C	HIS426
D	ILE9
D	GLY10
D	GLY12
D	LYS13
D	ILE32
D	GLU33
D	GLN34
D	MET38
D	GLY41
D	THR42
D	CYS43
D	GLY47
D	CYS48
D	LYS52
D	ALA99
D	ASN126
D	THR127
D	GLY128
D	ILE169
D	ARG252
D	SER258
D	GLY291
D	ASP292
D	GLN298
D	PHE299
D	THR300
D	TYR301
D	SER303

site_id	AF5
Number of Residues	1
Details	binding site for residue CU D 502

Chain	Residue
D	HIS260

site_id	AF6
Number of Residues	1
Details	binding site for residue CU D 503

Chain	Residue
D	HIS110

site_id	AF7
Number of Residues	1
Details	binding site for residue CU D 504

Chain	Residue
D	HIS227

site_id	AF8
Number of Residues	1
Details	binding site for residue CU D 505

Chain	Residue
D	HIS61

site_id	AF9
Number of Residues	2
Details	binding site for residue CU D 506

Chain	Residue
D	HIS56
D	GLN60

site_id	AG1
Number of Residues	1
Details	binding site for residue CU D 507

Chain	Residue
D	HIS84

site_id	AG2
Number of Residues	4
Details	binding site for residue CU D 508

Chain	Residue
C	HIS426
D	CYS43
D	CYS48
D	THR300

Functional Information from PROSITE/UniProt

site_id	PS00076
Number of Residues	11
Details	PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCIniGCIP

Chain	Residue	Details
A	GLY40-PRO50

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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