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6Y7E

Pseudomonas stutzeri nitrous oxide reductase mutant, H494A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0005507molecular_functioncopper ion binding
A0005509molecular_functioncalcium ion binding
A0016020cellular_componentmembrane
A0050304molecular_functionnitrous-oxide reductase activity
B0004129molecular_functioncytochrome-c oxidase activity
B0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0016020cellular_componentmembrane
B0050304molecular_functionnitrous-oxide reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FMT A 801
ChainResidue
APHE606
AVAL607
AB3P806
AHOH1079
AHOH1190

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 802
ChainResidue
AHOH1334
AHOH1368
AHIS326
AHIS382
AHIS433
AZN803

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 803
ChainResidue
AHIS130
AHIS433
AZN802
AHOH1334
AHOH1379

site_idAC4
Number of Residues9
Detailsbinding site for residue TRS A 804
ChainResidue
ATYR246
ATHR247
AASP333
AGLY334
AHOH920
AHOH954
AHOH1169
AHOH1221
AHOH1283

site_idAC5
Number of Residues6
Detailsbinding site for residue FMT A 805
ChainResidue
AASP119
ATHR170
AHOH907
AHOH1277
BFMT1301
BHOH1468

site_idAC6
Number of Residues13
Detailsbinding site for residue B3P A 806
ChainResidue
AARG114
AHIS590
AGLY591
ATHR605
AFMT801
AHOH929
AHOH940
AHOH985
AHOH1023
AHOH1070
AHOH1100
AHOH1293
BLYS122

site_idAC7
Number of Residues6
Detailsbinding site for residue NA A 807
ChainResidue
AMET168
AHOH1186
AHOH1201
AHOH1250
AHOH1383
AHOH1493

site_idAC8
Number of Residues6
Detailsbinding site for residue CL A 808
ChainResidue
AARG181
AASN241
AGLY327
ACYS328
AASN329
AHIS382

site_idAC9
Number of Residues6
Detailsbinding site for residue CUA A 809
ChainResidue
AHIS583
ACYS618
ATRP620
ACYS622
AHIS626
AMET629

site_idAD1
Number of Residues8
Detailsbinding site for residue FMT B 1301
ChainResidue
APHE123
AASN152
AFMT805
BASN589
BHOH1403
BHOH1451
BHOH1468
BHOH1712

site_idAD2
Number of Residues5
Detailsbinding site for residue ZN B 1302
ChainResidue
BHIS326
BHIS382
BHIS433
BHOH1447
BHOH1812

site_idAD3
Number of Residues12
Detailsbinding site for residue B3P B 1303
ChainResidue
ALYS122
BARG114
BHIS590
BGLY591
BTHR605
BFMT1304
BHOH1444
BHOH1446
BHOH1547
BHOH1580
BHOH1677
BHOH1724

site_idAD4
Number of Residues5
Detailsbinding site for residue FMT B 1304
ChainResidue
BPHE606
BVAL607
BB3P1303
BHOH1469
BHOH1485

site_idAD5
Number of Residues6
Detailsbinding site for residue NA B 1305
ChainResidue
BMET168
BHOH1628
BHOH1637
BHOH1700
BHOH1796
BHOH1883

site_idAD6
Number of Residues6
Detailsbinding site for residue CA B 1306
ChainResidue
BGLU259
BMET267
BASP273
BASN324
BHOH1443
BTYR256

site_idAD7
Number of Residues6
Detailsbinding site for residue CL B 1307
ChainResidue
BARG181
BASN241
BGLY327
BCYS328
BASN329
BHIS382

site_idAD8
Number of Residues6
Detailsbinding site for residue CUA B 1308
ChainResidue
BHIS583
BCYS618
BTRP620
BCYS622
BHIS626
BMET629

Functional Information from PROSITE/UniProt
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VsHgfvvvnhgvsmeispqqtssitfvadkpglhwyy......CswfChalHmeM
ChainResidueDetails
AVAL581-MET629

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS129
AHIS382
AHIS433
ALYS454
AGLU469
AALA494
AHIS583
ACYS618
ATRP620
ACYS622
AHIS626
AHIS130
AMET629
BHIS129
BHIS130
BHIS178
BTYR256
BGLU259
BMET267
BASP273
BASN324
BHIS326
AHIS178
BHIS382
BHIS433
BLYS454
BGLU469
BALA494
BHIS583
BCYS618
BTRP620
BCYS622
BHIS626
ATYR256
BMET629
AGLU259
AMET267
AASP273
AASN324
AHIS326

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PDB entries from 2025-07-02

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