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1PZS

Crystal Structure of a Cu-Zn Superoxide Dismutase from Mycobacterium tuberculosis at 1.63 resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0006801biological_processsuperoxide metabolic process
A0006979biological_processresponse to oxidative stress
A0009274cellular_componentpeptidoglycan-based cell wall
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0033194biological_processresponse to hydroperoxide
A0045454biological_processcell redox homeostasis
A0046872molecular_functionmetal ion binding
A0075136biological_processresponse to host
A0141082biological_processsymbiont-mediated detoxification of host-generated reactive oxygen species
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 172
ChainResidue
AHIS47
AHIS49
AHIS75
AHIS126
AHOH448

Functional Information from PROSITE/UniProt
site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GDAGkRvACgvI
ChainResidueDetails
AGLY157-ILE168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AHIS49
AVAL51
AHIS77
AGLY128

site_idSWS_FT_FI2
Number of Residues1
DetailsLIPID: S-diacylglycerol cysteine => ECO:0000305
ChainResidueDetails
ASER-34

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS75
AARG162

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS75

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PDB entries from 2024-07-24

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