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4G38

Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000103biological_processsulfate assimilation
A0004783molecular_functionsulfite reductase (NADPH) activity
A0008652biological_processamino acid biosynthetic process
A0009337cellular_componentsulfite reductase complex (NADPH)
A0016002molecular_functionsulfite reductase activity
A0016491molecular_functionoxidoreductase activity
A0019344biological_processcysteine biosynthetic process
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0050311molecular_functionsulfite reductase (ferredoxin) activity
A0050661molecular_functionNADP binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0070814biological_processhydrogen sulfide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 601
ChainResidue
AARG83
AARG117
AARG153
ALYS215
ALYS217
ASRM604
AHOH908

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 602
ChainResidue
AGLN396
AASN397
AHOH702
AHOH816
AILE362
AASN395

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 A 603
ChainResidue
ACYS434
ACYS440
AALA443
ATHR477
AGLY478
ACYS479
AASN481
AGLY482
ACYS483

site_idAC4
Number of Residues38
DetailsBINDING SITE FOR RESIDUE SRM A 604
ChainResidue
ALEU81
AARG83
AARG113
ATHR115
AASN116
AARG117
ATHR119
AGLN121
AHIS123
ALYS215
ALYS217
AGLY256
ALEU257
ASER258
AGLN396
AALA433
ACYS434
AVAL435
ATHR439
ACYS440
APRO441
ALEU442
AASN481
AGLY482
ACYS483
AARG485
APO4601
AHOH731
AHOH743
AHOH792
AHOH810
AHOH912
AHOH925
AHOH936
AHOH1108
AHOH1158
AHOH1205
AHOH1254

Functional Information from PROSITE/UniProt
site_idPS00365
Number of Residues17
DetailsNIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. TGCpngCgramlaEVGL
ChainResidueDetails
ATHR477-LEU493

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848
ChainResidueDetails
ACYS434
ACYS440
ACYS479

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848
ChainResidueDetails
ACYS483

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 398
ChainResidueDetails
AARG83activator
AARG153activator
ALYS215activator
ALYS217activator
ACYS434metal ligand
ACYS440metal ligand
ACYS479metal ligand
ACYS483electron shuttle, metal ligand

220113

PDB entries from 2024-05-22

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