Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6L3H

Cryo-EM structure of dimeric quinol dependent Nitric Oxide Reductase (qNOR) from the pathogen Neisseria meninigitidis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0009060biological_processaerobic respiration
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A1902600biological_processproton transmembrane transport
B0004129molecular_functioncytochrome-c oxidase activity
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue HEM A 801
ChainResidue
ATYR78
ATYR412
AALA634
AHIS635
ALEU638
AARG724
AASP728
AHEM802
ACA804
AGLN294
AGLY298
ATYR328
AARG332
AHIS335
AILE336
AALA339
AGLU411

site_idAC2
Number of Residues19
Detailsbinding site for residue HEM A 802
ChainResidue
ATYR78
AGLU411
ATYR412
ATRP486
AGLU494
AHIS541
AHIS542
AALA608
AGLY612
AILE615
AASN616
ASER630
AHIS633
AALA634
AALA637
ALEU638
ATYR642
AHEM801
ACA804

site_idAC3
Number of Residues4
Detailsbinding site for residue FE A 803
ChainResidue
AHIS490
AGLU494
AHIS541
AHIS542

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 804
ChainResidue
AGLY76
ATYR78
AGLU411
AHEM801
AHEM802

site_idAC5
Number of Residues17
Detailsbinding site for residue HEM B 801
ChainResidue
BTYR78
BGLN294
BGLY298
BTYR328
BARG332
BHIS335
BILE336
BALA339
BGLU411
BTYR412
BALA634
BHIS635
BLEU638
BARG724
BASP728
BHEM802
BCA804

site_idAC6
Number of Residues19
Detailsbinding site for residue HEM B 802
ChainResidue
BTYR78
BGLU411
BTYR412
BTRP486
BGLU494
BHIS541
BHIS542
BALA608
BGLY612
BILE615
BASN616
BSER630
BHIS633
BALA634
BALA637
BLEU638
BTYR642
BHEM801
BCA804

site_idAC7
Number of Residues4
Detailsbinding site for residue FE B 803
ChainResidue
BHIS490
BGLU494
BHIS541
BHIS542

site_idAC8
Number of Residues5
Detailsbinding site for residue CA B 804
ChainResidue
BGLY76
BTYR78
BGLU411
BHEM801
BHEM802

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues57
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWVVHLwVegffevfataafafvfynmgfvrrstatastlaaaaifmlggvpgtlHH
ChainResidueDetails
ATRP486-HIS542

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon