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1EM1

X-RAY CRYSTAL STRUCTURE FOR HUMAN MANGANESE SUPEROXIDE DISMUTASE, Q143A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0006801biological_processsuperoxide metabolic process
A0046872molecular_functionmetal ion binding
B0004784molecular_functionsuperoxide dismutase activity
B0006801biological_processsuperoxide metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 500
ChainResidue
ALYS178
BHIS2
BSER3
BHIS71
BHOH703

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AHOH708
ALYS1
AHIS2
ASER3
AHIS71

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 600
ChainResidue
AHIS26
AHIS74
AASP159
AHIS163
AHOH763

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 601
ChainResidue
BHIS26
BHIS74
BASP159
BHIS163
BHOH731

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY
ChainResidueDetails
AASP159-TYR166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
ChainResidueDetails
AHIS26
AHIS74
AASP159
AHIS163
BHIS26
BHIS74
BASP159
BHIS163

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:10334867, ECO:0000269|PubMed:16399855
ChainResidueDetails
ATYR34
BTYR34

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
ChainResidueDetails
ALYS44
ALYS51
ALYS98
ALYS106
BLYS44
BLYS51
BLYS98
BLYS106

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09671
ChainResidueDetails
ALYS90
ALYS178
BLYS90
BLYS178

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PDB entries from 2024-03-27

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