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1YV1

Fully reduced state of nigerythrin (all ferrous)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 301
ChainResidue
AGLU40
AGLU73
AHIS76
AGLU149
AHOH304

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 302
ChainResidue
AHOH356
AGLU73
AGLU115
AGLU149
AHIS152

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 303
ChainResidue
ACYS174
ACYS177
ACYS189
ACYS192

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 301
ChainResidue
BGLU40
BGLU73
BHIS76
BGLU149
BHOH304

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 302
ChainResidue
BGLU73
BGLU115
BGLU149
BHIS152
BHOH318

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 B 303
ChainResidue
BCYS174
BCYS177
BCYS189
BCYS192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues290
DetailsDomain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues66
DetailsDomain: {"description":"Rubredoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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