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3E4W

Crystal structure of a 33kDa catalase-related protein from Mycobacterium avium subsp. paratuberculosis. P2(1)2(1)2(1) crystal form.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042542biological_processresponse to hydrogen peroxide
A0042743biological_processhydrogen peroxide metabolic process
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A2000377biological_processregulation of reactive oxygen species metabolic process
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
B0042542biological_processresponse to hydrogen peroxide
B0042743biological_processhydrogen peroxide metabolic process
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
B2000377biological_processregulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
AARG25
APHE113
AGLY164
APHE270
AARG290
ATYR294
ASER297
AARG301
AHOH1256
AHOH1269
AALA26
ALEU27
AHIS28
AARG63
ASER98
AALA99
AGLN100
ALEU105

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 502
ChainResidue
BARG25
BALA26
BLEU27
BHIS28
BARG63
BSER98
BALA99
BGLN100
BPHE113
BHIS163
BGLY164
BPHE270
BARG290
BTYR294
BSER297
BARG301
BHOH1312
BHOH1457

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HEZ A 1100
ChainResidue
AHIS28
AGLN100
AALA102
ALEU104
ALEU105

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HEZ A 1110
ChainResidue
AARG103
AHIS183
AARG224
AILE246
BTHR187
BALA189

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HEZ B 1120
ChainResidue
ATHR187
AALA189
BARG103
BHIS183
BARG224

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HEZ A 1130
ChainResidue
AALA102
ALEU104
ALEU105
ALEU140
ALEU146
ASER238

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HEZ B 1140
ChainResidue
BHIS28
BGLN100
BALA102
BLEU105

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HEZ B 1150
ChainResidue
BLEU104
BLEU105
BARG139
BLEU147
BSER238

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 1200
ChainResidue
ASER107
ASER108
ATHR109
AHIS137

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 1210
ChainResidue
BSER107
BSER108
BTHR109
BGLY112
BHIS137
BHOH1417

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 1220
ChainResidue
AHIS137
APRO138
AARG139
ALEU140

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1230
ChainResidue
BHIS137
BPRO138
BARG139
BHOH1417

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 1240
ChainResidue
AHIS263
AGLY264

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1300
ChainResidue
APRO186
AGLU190
AARG224
BGLU161
BPRO186
BGLU190
BARG224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P04040
ChainResidueDetails
AHIS28
BHIS28

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATYR294
BTYR294

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PDB entries from 2024-07-10

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