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1N70

The Crystal Structure of Nitrite Reductase Mutant His287Ala from Rhodobacter Sphaeroides

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 401
ChainResidue
AHIS126
ACYS167
AHIS177
AMET182

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 402
ChainResidue
AHIS131
AHIS166
AHIS338
AHOH779

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ATHR224
AHOH636
AHOH803
AHOH804
AHOH805
AASP220

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AHOH806
AHOH807
AHOH808
AHOH809
AHOH810
AHOH811

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 503
ChainResidue
AHOH664
AHOH707
AHOH746
AHOH801
AHOH802
AHOH840

Functional Information from PROSITE/UniProt
site_idPS00283
Number of Residues17
DetailsSOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. LkDHEGKpVrYDtvYyI
ChainResidueDetails
ALEU194-ILE210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: type 1 copper site => ECO:0000250
ChainResidueDetails
AHIS126
ACYS167
AHIS177
AMET182

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: type 2 copper site => ECO:0000250
ChainResidueDetails
AHIS131
AHIS166
AHIS338

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ehk
ChainResidueDetails
AGLY97
APHE95

222926

PDB entries from 2024-07-24

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