Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6Y72

Pseudomonas stutzeri nitrous oxide reductase mutant, H178A

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 Residues11
Detailsbinding site for residue B3P A 701
ChainResidue
AARG114
BLYS122
BHOH956
AHIS590
AGLY591
ATHR605
AFMT708
AHOH808
AHOH836
AHOH869
AHOH918

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 702
ChainResidue
AMET168
AHOH979
AHOH1093
AHOH1128
AHOH1266
AHOH1304

site_idAC3
Number of Residues4
Detailsbinding site for residue NA A 703
ChainResidue
AASN173
AHOH1135
AHOH1367
AHOH1372

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 704
ChainResidue
ATYR256
AGLU259
AMET267
AASP273
AASN324
AHOH833

site_idAC5
Number of Residues4
Detailsbinding site for residue FMT A 705
ChainResidue
AHIS115
AGLY118
AHOH979
AHOH1234

site_idAC6
Number of Residues4
Detailsbinding site for residue FMT A 706
ChainResidue
AARG388
AASN390
ALYS403
AHOH854

site_idAC7
Number of Residues1
Detailsbinding site for residue FMT A 707
ChainResidue
AHOH1113

site_idAC8
Number of Residues6
Detailsbinding site for residue FMT A 708
ChainResidue
APHE606
AVAL607
AB3P701
AHOH808
AHOH882
AHOH1084

site_idAC9
Number of Residues6
Detailsbinding site for residue CL A 709
ChainResidue
AARG181
AASN241
AGLY327
ACYS328
AASN329
AHIS382

site_idAD1
Number of Residues6
Detailsbinding site for residue CUA A 710
ChainResidue
AHIS583
ACYS618
ATRP620
ACYS622
AHIS626
AMET629

site_idAD2
Number of Residues10
Detailsbinding site for residue B3P B 701
ChainResidue
ALYS122
AHOH999
BHIS590
BGLY591
BTHR605
BHOH838
BHOH924
BHOH933
BHOH1059
BHOH1123

site_idAD3
Number of Residues6
Detailsbinding site for residue CA B 702
ChainResidue
BTYR256
BGLU259
BMET267
BASP273
BASN324
BHOH840

site_idAD4
Number of Residues6
Detailsbinding site for residue K B 703
ChainResidue
AHOH829
AHOH920
BLYS454
BGLU469
BHOH817
BHOH992

site_idAD5
Number of Residues7
Detailsbinding site for residue FMT B 704
ChainResidue
ATRP615
BGLU196
BPHE197
BILE198
BASN238
BASN257
BHOH816

site_idAD6
Number of Residues2
Detailsbinding site for residue FMT B 705
ChainResidue
BASP511
BARG512

site_idAD7
Number of Residues3
Detailsbinding site for residue FMT B 706
ChainResidue
BMET135
BASP141
BTHR188

site_idAD8
Number of Residues6
Detailsbinding site for residue CUA B 707
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 Residues192
DetailsRegion: {"description":"COX2-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon