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

1L9E

Role of Histidine 269 in Catalysis by Monomeric Sarcosine Oxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008115molecular_functionsarcosine oxidase activity
A0016491molecular_functionoxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0005737cellular_componentcytoplasm
B0008115molecular_functionsarcosine oxidase activity
B0016491molecular_functionoxidoreductase activity
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 6402
ChainResidue
ATYR317
ATHR318
AGLY344
AFAD6400
AHOH6421

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 7402
ChainResidue
BHOH7408
BTYR317
BTHR318
BGLY344
BFAD7400

site_idAC3
Number of Residues40
DetailsBINDING SITE FOR RESIDUE FAD A 6400
ChainResidue
AGLY10
AGLY12
ASER13
AMET14
AVAL32
AASP33
AALA34
APHE35
AHIS39
AGLY42
ASER43
AHIS44
AARG49
AILE50
ATHR171
AARG172
AVAL173
ASER200
AMET201
AGLY202
ATRP204
ALEU208
AVAL225
ATYR254
ACYS315
AMET316
ATYR317
APHE342
AGLY344
AHIS345
AGLY346
APHE347
ALYS348
AIMD6401
ACL6402
AHOH6403
AHOH6410
AHOH6411
AHOH6413
AHOH6485

site_idAC4
Number of Residues40
DetailsBINDING SITE FOR RESIDUE FAD B 7400
ChainResidue
BGLY10
BGLY12
BSER13
BMET14
BVAL32
BASP33
BALA34
BPHE35
BHIS39
BGLY42
BSER43
BHIS44
BARG49
BILE50
BTHR171
BARG172
BVAL173
BSER200
BMET201
BGLY202
BTRP204
BLEU208
BVAL225
BTYR254
BCYS315
BMET316
BTYR317
BPHE342
BGLY344
BHIS345
BGLY346
BPHE347
BLYS348
BIMD7401
BCL7402
BHOH7403
BHOH7406
BHOH7412
BHOH7416
BHOH7456

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 6401
ChainResidue
AARG52
AMET245
AGLY344
ALYS348
AFAD6400
AHOH6420

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD B 7401
ChainResidue
BLYS348
BFAD7400
BHOH7435
BARG52
BMET245
BGLY344

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues60
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"S-8alpha-FAD cysteine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 2gb0
ChainResidueDetails
AHIS269
ACYS315
AARG49
AHIS45

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 2gb0
ChainResidueDetails
BHIS269
BCYS315
BARG49
BHIS45

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2gb0
ChainResidueDetails
AGLY344

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2gb0
ChainResidueDetails
BGLY344

site_idMCSA1
Number of Residues7
DetailsM-CSA 113
ChainResidueDetails
AHIS45electrostatic stabiliser
ATHR48hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AARG49electrostatic stabiliser, modifies pKa
ALYS265hydrogen bond donor, proton acceptor, proton donor, proton relay
AHIS269hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ACYS315activator, alter redox potential, covalently attached
ALYS348electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues7
DetailsM-CSA 113
ChainResidueDetails
BHIS45electrostatic stabiliser
BTHR48hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BARG49electrostatic stabiliser, modifies pKa
BLYS265hydrogen bond donor, proton acceptor, proton donor, proton relay
BHIS269hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BCYS315activator, alter redox potential, covalently attached
BLYS348electrostatic stabiliser, hydrogen bond donor

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon