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4AX3

Structure of three-domain heme-Cu nitrite reductase from Ralstonia pickettii at 1.6 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0005507molecular_functioncopper ion binding
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
C0005507molecular_functioncopper ion binding
C0009055molecular_functionelectron transfer activity
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0050421molecular_functionnitrite reductase (NO-forming) activity
D0005507molecular_functioncopper ion binding
D0009055molecular_functionelectron transfer activity
D0016491molecular_functionoxidoreductase activity
D0020037molecular_functionheme binding
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
D0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 501
ChainResidue
AHIS94
ACYS135
AHIS143
AMET148

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 502
ChainResidue
AHIS99
AHIS134
AHIS289
AHOH2424

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 600
ChainResidue
ATHR363
ACYS364
ACYS367
AHIS368
APRO380
APRO381
ALEU382
ASER385
APHE387
AILE398
AVAL399
ALEU403
AASN404
AGLY405
AVAL409
ASER416
AMET418
AMET421
AMET92

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 501
ChainResidue
BHIS94
BCYS135
BHIS143
BMET148

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 502
ChainResidue
BHIS99
BHIS134
BHIS289
BHOH2230
BHOH2459

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 600
ChainResidue
BMET92
BTHR363
BCYS364
BCYS367
BHIS368
BPRO380
BPRO381
BLEU382
BSER385
BPHE387
BLEU403
BASN404
BGLY405
BSER416
BMET418
BMET421

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 501
ChainResidue
CHIS94
CCYS135
CHIS143
CMET148

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 502
ChainResidue
CHIS99
CHIS134
CHIS289
CHOH2244

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM C 600
ChainResidue
CTHR363
CCYS364
CVAL366
CCYS367
CHIS368
CPRO380
CPRO381
CLEU382
CSER385
CPHE387
CLEU403
CASN404
CGLY405
CSER416
CVAL417
CMET418
CMET421

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 501
ChainResidue
DHIS94
DCYS135
DHIS143
DMET148

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 502
ChainResidue
DHIS99
DHIS134
DHIS289
DHOH2176

site_idBC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM D 600
ChainResidue
DMET418
DMET421
DMET92
DTHR363
DCYS364
DCYS367
DHIS368
DPRO380
DPRO381
DLEU382
DSER385
DPHE387
DILE398
DASN404
DGLY405
DSER416

225946

PDB entries from 2024-10-09

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