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3SID

Crystal structure of oxidized Symerythrin from Cyanophora paradoxa, azide adduct at 50% occupancy

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 Residues7
DetailsBINDING SITE FOR RESIDUE FE A 200
ChainResidue
AGLU71
AGLU128
AGLU162
AHIS165
AHOH183
AFE201
AAZI300

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FE A 201
ChainResidue
AGLU71
AGLU131
AGLU162
AHOH183
AFE200
AHOH204
AAZI300
AGLU37
AGLU40

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AZI A 300
ChainResidue
AGLU40
AGLU71
AVAL127
AGLU128
AGLU131
AGLU162
AHOH183
AFE200
AFE201
AHOH204

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FE B 200
ChainResidue
BGLU37
BGLU40
BGLU71
BGLU131
BGLU162
BHOH181
BHOH198
BFE201
BAZI300

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE B 201
ChainResidue
BGLU71
BGLU128
BGLU162
BHIS165
BHOH181
BFE200
BAZI300

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AZI B 300
ChainResidue
BGLU40
BGLU71
BVAL127
BGLU128
BGLU131
BGLU162
BHOH181
BHOH198
BFE200
BFE201

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 2024-07-24

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