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1AOP

SULFITE REDUCTASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION

Replaces:  1GEO
Functional Information from GO Data
ChainGOidnamespacecontents
A0004783molecular_functionsulfite reductase (NADPH) activity
A0008652biological_processamino acid biosynthetic process
A0009337cellular_componentsulfite reductase complex (NADPH)
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0050661molecular_functionNADP binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 585
ChainResidue
ALYS217
ASRM580
AHOH709
AARG83
AARG117
AARG153
ALYS215

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 590
ChainResidue
AILE362
AASN395
AGLN396
AASN397
AHOH640
AHOH642

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 575
ChainResidue
ACYS434
ACYS440
AALA443
ATHR477
ACYS479
AASN481
ACYS483
ASRM580

site_idAC4
Number of Residues41
DetailsBINDING SITE FOR RESIDUE SRM A 580
ChainResidue
AARG83
AARG113
ATHR115
AASN116
AARG117
ATHR119
AGLN121
AHIS123
AARG214
ALYS215
ALYS217
AGLY256
ALEU257
ASER258
AGLN396
AALA433
ACYS434
AVAL435
ATHR439
ACYS440
APRO441
AASN481
AGLY482
ACYS483
AARG485
ASF4575
APO4585
AHOH607
AHOH694
AHOH695
AHOH717
AHOH743
AHOH771
AHOH772
AHOH773
AHOH774
AHOH827
AHOH832
AHOH887
AHOH901
AHOH966

site_idACT
Number of Residues4
DetailsFOUR ACTIVE SITE RESIDUES THAT CONTACT THE BOUND PHOSPHATE.
ChainResidue
AARG83
AARG153
ALYS215
ALYS217

site_idBRG
Number of Residues1
DetailsCYSTEINE THIOLATE IN THE ACTIVE CENTER THAT BRIDGES THE HEME IRON TO THE [4FE-4S] CLUSTER.
ChainResidue
ACYS483

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
AVAL435
APRO441
APRO480

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848
ChainResidueDetails
AGLY484

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 9315848, 7569952, 10984484, 9315849, 15966732
ChainResidueDetails
ALYS215
AARG83
ACYS483
ALYS217
AARG153

site_idMCSA1
Number of Residues8
DetailsM-CSA 398
ChainResidueDetails
ACYS84activator
AASN154activator
APHE216activator
ATHR218activator
AVAL435metal ligand
APRO441metal ligand
APRO480metal ligand
AGLY484electron shuttle, metal ligand

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PDB entries from 2024-07-24

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