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3QHC

Crystal structure of Symerythrin from Cyanophora paradoxa, reduced with dithionite

Functional Information from GO Data
ChainGOidnamespacecontents
A0009842cellular_componentcyanelle
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0009842cellular_componentcyanelle
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FE A 182
ChainResidue
AGLU37
AGLU40
AGLU71
AGLU131
AGLU162
AFE181
AFE183
AHOH204
AHOH339

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 181
ChainResidue
AGLU71
AGLU128
AGLU162
AHIS165
AFE182
AHOH204

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 183
ChainResidue
AGLU37
AGLU71
AHIS74
AGLU162
AFE182
AHOH339

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FE B 182
ChainResidue
BGLU37
BGLU40
BGLU71
BGLU131
BGLU162
BFE181
BFE183
BHOH224
BHOH293

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 183
ChainResidue
BGLU37
BGLU71
BHIS74
BGLU162
BFE182
BHOH293

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 181
ChainResidue
BGLU71
BGLU128
BGLU162
BHIS165
BFE182
BHOH224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU71
AHIS74
AGLU162
AHIS165
BGLU71
BHIS74
BGLU162
BHIS165

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PDB entries from 2024-07-10

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