Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5H8Y

Crystal structure of the complex between maize sulfite reductase and ferredoxin in the form-2 crystal

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000103	biological_process	sulfate assimilation
A	0003677	molecular_function	DNA binding
A	0003690	molecular_function	double-stranded DNA binding
A	0009507	cellular_component	chloroplast
A	0009532	cellular_component	plastid stroma
A	0009536	cellular_component	plastid
A	0009570	cellular_component	chloroplast stroma
A	0016491	molecular_function	oxidoreductase activity
A	0019418	biological_process	sulfide oxidation
A	0020037	molecular_function	heme binding
A	0042644	cellular_component	chloroplast nucleoid
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046872	molecular_function	metal ion binding
A	0050311	molecular_function	sulfite reductase (ferredoxin) activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	1900160	biological_process	plastid chromosome packaging
B	0000103	biological_process	sulfate assimilation
B	0003677	molecular_function	DNA binding
B	0003690	molecular_function	double-stranded DNA binding
B	0009507	cellular_component	chloroplast
B	0009532	cellular_component	plastid stroma
B	0009536	cellular_component	plastid
B	0009570	cellular_component	chloroplast stroma
B	0016491	molecular_function	oxidoreductase activity
B	0019418	biological_process	sulfide oxidation
B	0020037	molecular_function	heme binding
B	0042644	cellular_component	chloroplast nucleoid
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0046872	molecular_function	metal ion binding
B	0050311	molecular_function	sulfite reductase (ferredoxin) activity
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	1900160	biological_process	plastid chromosome packaging
C	0000103	biological_process	sulfate assimilation
C	0003677	molecular_function	DNA binding
C	0003690	molecular_function	double-stranded DNA binding
C	0009507	cellular_component	chloroplast
C	0009532	cellular_component	plastid stroma
C	0009536	cellular_component	plastid
C	0009570	cellular_component	chloroplast stroma
C	0016491	molecular_function	oxidoreductase activity
C	0019418	biological_process	sulfide oxidation
C	0020037	molecular_function	heme binding
C	0042644	cellular_component	chloroplast nucleoid
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0046872	molecular_function	metal ion binding
C	0050311	molecular_function	sulfite reductase (ferredoxin) activity
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	1900160	biological_process	plastid chromosome packaging
D	0000103	biological_process	sulfate assimilation
D	0003677	molecular_function	DNA binding
D	0003690	molecular_function	double-stranded DNA binding
D	0009507	cellular_component	chloroplast
D	0009532	cellular_component	plastid stroma
D	0009536	cellular_component	plastid
D	0009570	cellular_component	chloroplast stroma
D	0016491	molecular_function	oxidoreductase activity
D	0019418	biological_process	sulfide oxidation
D	0020037	molecular_function	heme binding
D	0042644	cellular_component	chloroplast nucleoid
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0046872	molecular_function	metal ion binding
D	0050311	molecular_function	sulfite reductase (ferredoxin) activity
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	1900160	biological_process	plastid chromosome packaging
E	0009055	molecular_function	electron transfer activity
E	0022900	biological_process	electron transport chain
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0009055	molecular_function	electron transfer activity
F	0022900	biological_process	electron transport chain
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue SF4 A 701

Chain	Residue
A	CYS494
A	CYS500
A	ALA503
A	CYS540
A	ASN542
A	CYS544

site_id	AC2
Number of Residues	37
Details	binding site for residue SRM A 702

Chain	Residue
A	ARG153
A	THR155
A	THR156
A	ARG157
A	THR159
A	GLN161
A	HIS163
A	ARG275
A	LYS276
A	LYS278
A	GLY318
A	MET319
A	GLY320
A	ARG368
A	GLN454
A	ALA493
A	CYS494
A	PRO495
A	CYS500
A	PRO501
A	LEU502
A	ASN542
A	GLY543
A	CYS544
A	ARG546
A	CL704
A	HOH803
A	HOH805
A	HOH811
A	HOH821
A	HOH825
A	HOH876
A	HOH892
A	HOH898
A	TYR106
A	GLN108
A	ARG124

site_id	AC3
Number of Residues	6
Details	binding site for residue MG A 703

Chain	Residue
A	VAL424
A	ASN453
A	ASN455
A	HOH842
A	HOH866
A	HOH873

site_id	AC4
Number of Residues	4
Details	binding site for residue CL A 704

Chain	Residue
A	ARG193
A	LYS276
A	LYS278
A	SRM702

site_id	AC5
Number of Residues	6
Details	binding site for residue SF4 B 701

Chain	Residue
B	CYS494
B	CYS500
B	ALA503
B	CYS540
B	ASN542
B	CYS544

site_id	AC6
Number of Residues	37
Details	binding site for residue SRM B 702

Chain	Residue
B	TYR106
B	GLN108
B	ARG124
B	ARG153
B	THR155
B	THR156
B	ARG157
B	THR159
B	GLN161
B	HIS163
B	ARG275
B	LYS276
B	LYS278
B	GLY318
B	MET319
B	GLY320
B	ARG368
B	GLN454
B	ALA493
B	CYS494
B	PRO495
B	LEU499
B	CYS500
B	LEU502
B	ASN542
B	GLY543
B	CYS544
B	ARG546
B	CL704
B	HOH803
B	HOH805
B	HOH817
B	HOH846
B	HOH863
B	HOH894
B	HOH901
B	HOH902

site_id	AC7
Number of Residues	5
Details	binding site for residue MG B 703

Chain	Residue
B	HOH827
B	HOH834
B	VAL424
B	ASN453
B	ASN455

site_id	AC8
Number of Residues	5
Details	binding site for residue CL B 704

Chain	Residue
B	ARG124
B	ARG193
B	LYS276
B	LYS278
B	SRM702

site_id	AC9
Number of Residues	6
Details	binding site for residue SF4 C 701

Chain	Residue
C	CYS494
C	CYS500
C	ALA503
C	CYS540
C	ASN542
C	CYS544

site_id	AD1
Number of Residues	34
Details	binding site for residue SRM C 702

Chain	Residue
C	TYR106
C	GLN108
C	ARG124
C	ARG153
C	THR155
C	THR156
C	ARG157
C	THR159
C	GLN161
C	HIS163
C	ARG275
C	LYS276
C	LYS278
C	GLY318
C	MET319
C	GLY320
C	ARG368
C	GLN454
C	ALA493
C	CYS494
C	PRO495
C	CYS500
C	PRO501
C	LEU502
C	ASN542
C	GLY543
C	CYS544
C	ARG546
C	CL704
C	HOH812
C	HOH838
C	HOH840
C	HOH843
C	HOH865

site_id	AD2
Number of Residues	6
Details	binding site for residue MG C 703

Chain	Residue
C	VAL424
C	ASN453
C	ASN455
C	HOH815
C	HOH824
C	HOH830

site_id	AD3
Number of Residues	4
Details	binding site for residue CL C 704

Chain	Residue
C	ARG193
C	LYS276
C	LYS278
C	SRM702

site_id	AD4
Number of Residues	7
Details	binding site for residue SF4 D 701

Chain	Residue
D	CYS494
D	CYS500
D	ALA503
D	THR538
D	CYS540
D	ASN542
D	CYS544

site_id	AD5
Number of Residues	30
Details	binding site for residue SRM D 702

Chain	Residue
D	TYR106
D	GLN108
D	ARG124
D	ARG153
D	THR155
D	THR156
D	ARG157
D	THR159
D	GLN161
D	HIS163
D	ARG275
D	LYS276
D	LYS278
D	GLY318
D	MET319
D	GLY320
D	ARG368
D	GLN454
D	ALA493
D	CYS494
D	PRO495
D	CYS500
D	PRO501
D	ASN542
D	GLY543
D	CYS544
D	ARG546
D	CL704
D	HOH816
D	HOH840

site_id	AD6
Number of Residues	5
Details	binding site for residue MG D 703

Chain	Residue
D	VAL424
D	ASN453
D	ASN455
D	HOH802
D	HOH805

site_id	AD7
Number of Residues	3
Details	binding site for residue CL D 704

Chain	Residue
D	ARG193
D	LYS276
D	SRM702

site_id	AD8
Number of Residues	8
Details	binding site for residue FES E 101

Chain	Residue
E	SER38
E	CYS39
E	ARG40
E	GLY42
E	SER43
E	CYS44
E	CYS47
E	CYS77

site_id	AD9
Number of Residues	9
Details	binding site for residue FES F 101

Chain	Residue
F	SER38
F	CYS39
F	ARG40
F	GLY42
F	SER43
F	CYS44
F	SER46
F	CYS47
F	CYS77

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGSCSSC

Chain	Residue	Details
E	CYS39-CYS47

site_id	PS00365
Number of Residues	17
Details	NIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. TGCpngCarpymaELGF

Chain	Residue	Details
A	THR538-PHE554

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	66
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	90
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

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