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6TFD

Crystal structure of nitrite and NO bound three-domain copper-containing nitrite reductase from Hyphomicrobium denitrificans strain 1NES1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005507molecular_functioncopper ion binding
A0006807biological_processobsolete nitrogen compound metabolic process
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0004322molecular_functionferroxidase activity
B0005507molecular_functioncopper ion binding
B0006807biological_processobsolete nitrogen compound metabolic process
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
C0004322molecular_functionferroxidase activity
C0005507molecular_functioncopper ion binding
C0006807biological_processobsolete nitrogen compound metabolic process
C0009055molecular_functionelectron transfer activity
C0016491molecular_functionoxidoreductase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0046872molecular_functionmetal ion binding
C0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 501
ChainResidue
AHIS222
ACYS263
AHIS271
AMET276

site_idAC2
Number of Residues5
Detailsbinding site for residue CU A 502
ChainResidue
AASP225
AHIS227
AHIS262
ANO2504
CHIS419

site_idAC3
Number of Residues5
Detailsbinding site for residue CU A 503
ChainResidue
AGLN79
AHIS80
ACYS117
AHIS122
AMET127

site_idAC4
Number of Residues7
Detailsbinding site for residue NO2 A 504
ChainResidue
AASP225
AHIS227
AHIS262
ACU502
CHIS368
CILE370
CHIS419

site_idAC5
Number of Residues7
Detailsbinding site for residue NO2 A 505
ChainResidue
AHIS368
AILE370
AHIS419
BASP225
BHIS227
BHIS262
BCU502

site_idAC6
Number of Residues5
Detailsbinding site for residue CU B 501
ChainResidue
BHIS222
BCYS263
BTHR265
BHIS271
BMET276

site_idAC7
Number of Residues4
Detailsbinding site for residue CU B 502
ChainResidue
AHIS419
ANO2505
BHIS227
BHIS262

site_idAC8
Number of Residues5
Detailsbinding site for residue CU B 503
ChainResidue
BGLN79
BHIS80
BCYS117
BHIS122
BMET127

site_idAC9
Number of Residues7
Detailsbinding site for residue NO B 504
ChainResidue
BHIS368
BILE370
BHIS419
CASP225
CHIS227
CHIS262
CCU502

site_idAD1
Number of Residues4
Detailsbinding site for residue CU C 501
ChainResidue
CHIS222
CCYS263
CHIS271
CMET276

site_idAD2
Number of Residues5
Detailsbinding site for residue CU C 502
ChainResidue
BHIS419
BNO504
CASP225
CHIS227
CHIS262

site_idAD3
Number of Residues5
Detailsbinding site for residue CU C 503
ChainResidue
CGLN79
CHIS80
CCYS117
CHIS122
CMET127

Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GqFdYyCsLPghRqAGMqgvL
ChainResidueDetails
AGLY111-LEU131

219869

PDB entries from 2024-05-15

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