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1SY7

Crystal structure of the catalase-1 from Neurospora crassa, native structure at 1.75A resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005619cellular_componentascospore wall
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0048315biological_processconidium formation
A0098869biological_processcellular oxidant detoxification
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005619cellular_componentascospore wall
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0048315biological_processconidium formation
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HDD A 1880
ChainResidue
AARG89
APHE170
APHE178
AVAL238
AASN239
APHE355
ALEU371
AGLY374
AARG375
ASER378
ATYR379
AVAL90
ATHR382
AGLN383
AHOH1887
AHOH2318
AHOH2352
AVAL91
AHIS92
AARG129
AGLY148
AVAL163
AGLY164
AASN165

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HDD B 1881
ChainResidue
BARG89
BVAL90
BVAL91
BHIS92
BARG129
BGLY148
BVAL163
BGLY164
BASN165
BPHE170
BPHE178
BVAL238
BASN239
BPHE355
BLEU371
BGLY374
BARG375
BSER378
BTYR379
BTHR382
BGLN383
BHOH1891
BHOH1920
BHOH1952

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM B 1882
ChainResidue
BILE78
BASP82
BARG89
BVAL90
BVAL91
BHIS92
BARG129
BGLY148
BVAL163
BGLY164
BASN165
BALA175
BPHE178
BVAL238
BASN239
BPHE355
BLEU371
BARG375
BSER378
BTYR379
BTHR382
BGLN383
BARG386
BHOH1891
BHOH1920
BHOH1952

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM A 1883
ChainResidue
AHOH2352
AILE78
AASP82
AARG89
AVAL90
AVAL91
AHIS92
AARG129
AGLY148
AVAL163
AGLY164
AASN165
AALA175
APHE178
AVAL238
AASN239
APHE355
ALEU371
AARG375
ASER378
ATYR379
ATHR382
AGLN383
AARG386
AHOH1887
AHOH2318

Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RNFSYfDTQ
ChainResidueDetails
AARG375-GLN383

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdHeripERvvHarGSG
ChainResidueDetails
APHE81-GLY97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15342250","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15342250","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"15342250","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsCross-link: {"description":"3-(S-cysteinyl)-tyrosine (Cys-Tyr)","evidences":[{"source":"PubMed","id":"15342250","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
AHIS92
ASER131
AASN165

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
BHIS92
BSER131
BASN165

249697

PDB entries from 2026-02-25

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