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2PPD

Oxidized H145A mutant of AfNiR bound to nitric oxide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0019333biological_processdenitrification pathway
A0042128biological_processnitrate assimilation
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
B0019333biological_processdenitrification pathway
B0042128biological_processnitrate assimilation
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
C0005507molecular_functioncopper ion binding
C0016491molecular_functionoxidoreductase activity
C0019333biological_processdenitrification pathway
C0042128biological_processnitrate assimilation
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU1 A 501
ChainResidue
AHIS95
ACYS136
AMET150

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 502
ChainResidue
AHIS100
AHIS135
ANO503
BHIS306

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU1 B 501
ChainResidue
BMET150
BHIS95
BCYS136

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 502
ChainResidue
BHIS100
BHIS135
BNO503
CHIS306

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU1 C 501
ChainResidue
CHIS95
CCYS136
CMET150

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 502
ChainResidue
AHIS306
CHIS100
CHIS135
CHOH503

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 1503
ChainResidue
BGLY229
BHIS319

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO A 503
ChainResidue
AASP98
AHIS100
AHIS135
ACU502
BHIS255
BILE257
BHIS306

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO B 503
ChainResidue
BASP98
BHIS100
BHIS135
BCU502
CHIS255
CILE257
CHIS306

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TRS A 1501
ChainResidue
ATHR212
ALEU213
ATHR214
AHOH1633
AHOH1667
AHOH1671
BTHR212
BLEU213
BTHR214
CTHR212
CLEU213
CTHR214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"description":"type 2 copper site"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"description":"type 1 copper site"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues164
DetailsDomain: {"description":"Plastocyanin-like 2"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
AASP98
AHIS255

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
BASP98
BHIS255

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
CASP98
CHIS255

238895

PDB entries from 2025-07-16

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