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4BIM

CATALASE 3 FROM NEUROSPORA CRASSA IN TETRAGONAL FORM EXPOSES A MODIFIED TETRAMERIC ORGANIZATION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
B0004096molecular_functioncatalase activity
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
C0004096molecular_functioncatalase activity
C0006979biological_processresponse to oxidative stress
C0020037molecular_functionheme binding
D0004096molecular_functioncatalase activity
D0006979biological_processresponse to oxidative stress
D0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 4000
ChainResidue
AARG99
APHE180
APHE188
AILE248
AHIS249
APHE365
ALEU381
AGLY384
AARG385
ASER388
ATYR389
AVAL100
ATHR392
AGLN393
AARG396
BLEU88
AVAL101
AHIS102
AARG139
AGLY158
AVAL173
AGLY174
AASN175

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 4000
ChainResidue
ALEU88
BARG99
BVAL100
BVAL101
BHIS102
BARG139
BGLY158
BALA160
BVAL173
BGLY174
BASN175
BPHE180
BPHE188
BILE248
BHIS249
BPHE365
BLEU381
BGLY384
BARG385
BSER388
BTYR389
BTHR392
BGLN393
BARG396

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM C 4000
ChainResidue
CARG99
CVAL100
CVAL101
CHIS102
CARG139
CALA160
CVAL173
CGLY174
CASN175
CPHE180
CPHE188
CILE248
CHIS249
CPHE365
CLEU381
CGLY384
CARG385
CSER388
CTYR389
CTHR392
CGLN393
CARG396

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM D 4000
ChainResidue
CLEU88
CASP92
DARG99
DVAL100
DHIS102
DARG139
DSER141
DALA160
DVAL173
DGLY174
DASN175
DPHE180
DALA185
DPHE188
DILE248
DHIS249
DLEU381
DARG385
DSER388
DTYR389
DTHR392
DGLN393
DARG396

Functional Information from PROSITE/UniProt
site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdHeripERvvHarGAG
ChainResidueDetails
APHE91-GLY107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
ChainResidueDetails
AHIS102
AASN175
BHIS102
BASN175
CHIS102
CASN175
DHIS102
DASN175

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
ATYR389
BTYR389
CTYR389
DTYR389

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PDB entries from 2024-10-16

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