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3O0R

Crystal structure of nitric oxide reductase from Pseudomonas aeruginosa in complex with antibody fragment

Functional Information from GO Data
ChainGOidnamespacecontents
B0004129molecular_functioncytochrome-c oxidase activity
B0005886cellular_componentplasma membrane
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016966molecular_functionnitric oxide reductase activity
B0019333biological_processdenitrification pathway
B0020037molecular_functionheme binding
B0022904biological_processrespiratory electron transport chain
B0046872molecular_functionmetal ion binding
B1902600biological_processproton transmembrane transport
C0005886cellular_componentplasma membrane
C0009055molecular_functionelectron transfer activity
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM B 801
ChainResidue
BGLN30
BGLU135
BHIS349
BPHE352
BTYR353
BILE400
BARG440
BGLY444
BHEM802
CALA72
CTYR73
BGLY34
CPHE74
CCA804
BLEU35
BMET37
BTYR41
BPHE53
BARG57
BHIS60
BLEU64

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 802
ChainResidue
BGLU135
BPHE136
BTRP203
BVAL210
BGLU211
BHIS258
BHIS259
BGLU280
BALA322
BGLY326
BPHE327
BHIS329
BTHR330
BASN335
BHIS339
BGLY340
BTHR344
BHIS347
BTYR356
BHEM801
BO805
BHOH906
BHOH931
CCA804

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 803
ChainResidue
BHIS207
BGLU211
BHIS258
BHIS259
BO805

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA C 804
ChainResidue
BARG57
BGLU135
BHEM801
BHEM802
BHOH906
CGLY71
CTYR73

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE O B 805
ChainResidue
BGLU211
BHIS258
BHIS259
BHEM802
BFE803

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC C 201
ChainResidue
BASN54
CASN59
CCYS61
CCYS64
CHIS65
CALA75
CVAL81
CARG84
CTRP98
CMET99
CARG109
CARG110
CALA111
CMET112
CPRO113
CPHE115
CLEU125
CHOH305
CHOH309
CHOH330
CHOH332

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues57
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWVVHLwVegvwelimgailafvlvkitgvdreviekwlyviiamalisgiigtgHH
ChainResidueDetails
BTRP203-HIS259

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Signal-anchor","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-10-08

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