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1GG9

CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, HIS128ASN VARIANT.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006972biological_processhyperosmotic response
A0006974biological_processDNA damage response
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006972biological_processhyperosmotic response
B0006974biological_processDNA damage response
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042744biological_processhydrogen peroxide catabolic process
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
C0004096molecular_functioncatalase activity
C0004601molecular_functionperoxidase activity
C0005506molecular_functioniron ion binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006972biological_processhyperosmotic response
C0006974biological_processDNA damage response
C0006979biological_processresponse to oxidative stress
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0042744biological_processhydrogen peroxide catabolic process
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0098869biological_processcellular oxidant detoxification
D0004096molecular_functioncatalase activity
D0004601molecular_functionperoxidase activity
D0005506molecular_functioniron ion binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006972biological_processhyperosmotic response
D0006974biological_processDNA damage response
D0006979biological_processresponse to oxidative stress
D0016491molecular_functionoxidoreductase activity
D0020037molecular_functionheme binding
D0042744biological_processhydrogen peroxide catabolic process
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 760
ChainResidue
AARG125
APHE214
AILE274
AHIS275
APHE391
ALEU407
AARG411
ASER414
ATYR415
ATHR418
AGLN419
AILE126
AARG422
AHOH781
AHOH827
AHOH856
AHOH1143
DASP118
AVAL127
AASN128
AARG165
AGLY184
AVAL199
AGLY200
AASN201

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 760
ChainResidue
BARG125
BILE126
BVAL127
BASN128
BARG165
BGLY184
BVAL199
BGLY200
BASN201
BPHE214
BILE274
BHIS275
BPHE391
BLEU407
BARG411
BSER414
BTYR415
BTHR418
BGLN419
BARG422
BHOH836
BHOH859
BHOH903
BHOH933
CASP118

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM C 760
ChainResidue
BASP118
CARG125
CILE126
CVAL127
CASN128
CARG165
CGLY184
CVAL199
CGLY200
CASN201
CPHE214
CHIS275
CPHE391
CLEU407
CARG411
CSER414
CTYR415
CTHR418
CGLN419
CARG422
CHOH890
CHOH935
CHOH965
CHOH1246

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM D 760
ChainResidue
AASP118
DARG125
DILE126
DVAL127
DASN128
DARG165
DGLY184
DVAL199
DGLY200
DASN201
DPHE214
DILE274
DHIS275
DPHE391
DLEU407
DARG411
DSER414
DTYR415
DTHR418
DGLN419
DARG422
DHOH960
DHOH985
DHOH1031
DHOH1062

Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFSYtDTQ
ChainResidueDetails
AARG411-GLN419

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
ChainResidueDetails
AASN128
AASN201
BASN128
BASN201
CASN128
CASN201
DASN128
DASN201

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
ATYR415
BTYR415
CTYR415
DTYR415

site_idSWS_FT_FI3
Number of Residues8
DetailsCROSSLNK: 3'-histidyl-3-tyrosine (His-Tyr)
ChainResidueDetails
AHIS392
ATYR415
BHIS392
BTYR415
CHIS392
CTYR415
DHIS392
DTYR415

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 573
ChainResidueDetails
AASN128proton shuttle (general acid/base)
AASN201electrostatic stabiliser
AHIS392proton shuttle (general acid/base)

site_idMCSA2
Number of Residues3
DetailsM-CSA 573
ChainResidueDetails
BASN128proton shuttle (general acid/base)
BASN201electrostatic stabiliser
BHIS392proton shuttle (general acid/base)

site_idMCSA3
Number of Residues3
DetailsM-CSA 573
ChainResidueDetails
CASN128proton shuttle (general acid/base)
CASN201electrostatic stabiliser
CHIS392proton shuttle (general acid/base)

site_idMCSA4
Number of Residues3
DetailsM-CSA 573
ChainResidueDetails
DASN128proton shuttle (general acid/base)
DASN201electrostatic stabiliser
DHIS392proton shuttle (general acid/base)

217705

数据于2024-03-27公开中

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