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2JBV

Crystal structure of choline oxidase reveals insights into the catalytic mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0019285biological_processglycine betaine biosynthetic process from choline
A0033713molecular_functioncholine:oxygen 1-oxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0019285biological_processglycine betaine biosynthetic process from choline
B0033713molecular_functioncholine:oxygen 1-oxidoreductase activity
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues46
DetailsBINDING SITE FOR RESIDUE FAO A1528
ChainResidue
AGLY20
AALA90
ALYS91
AVAL92
AGLY95
ACYS96
ASER97
AHIS99
AASN100
ASER101
ACYS102
AGLY22
AILE103
ALEU230
AARG231
AALA232
ASER268
ATHR269
AGLY270
AASP273
AVAL464
ATYR465
ASER23
AHIS466
AASP499
AALA500
AASN510
APRO511
AASN512
AVAL515
ADMS1530
AHOH2292
AHOH2450
AALA24
AHOH2480
AHOH2481
AHOH2482
AHOH2483
AHOH2484
AUNX2500
AUNX2501
AGLU44
AALA45
ATRP71
AALA88
AARG89

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A1530
ChainResidue
ASER101
AILE103
AHIS351
AVAL464
ATYR465
AFAO1528
AUNX2500
AUNX2501

site_idAC3
Number of Residues47
DetailsBINDING SITE FOR RESIDUE FAO B1531
ChainResidue
BUNX2500
BUNX2501
BGLY20
BGLY22
BSER23
BALA24
BGLU44
BALA45
BTRP71
BALA88
BARG89
BALA90
BLYS91
BVAL92
BGLY95
BCYS96
BSER97
BHIS99
BASN100
BSER101
BCYS102
BILE103
BLEU230
BARG231
BALA232
BSER268
BTHR269
BGLY270
BASP273
BLEU277
BVAL464
BTYR465
BHIS466
BASP499
BALA500
BASN510
BPRO511
BASN512
BVAL515
BDMS1533
BHOH2078
BHOH2265
BHOH2451
BHOH2473
BHOH2482
BHOH2483
BHOH2484

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS B1533
ChainResidue
BTRP61
BSER101
BILE103
BTRP331
BHIS351
BVAL464
BFAO1531
BUNX2501

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX A2500
ChainResidue
AHIS466
AASN510
AFAO1528
ADMS1530
AUNX2501

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNX A2501
ChainResidue
AVAL464
AHIS466
AASN510
AFAO1528
ADMS1530
AUNX2500

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX B2500
ChainResidue
BHIS466
BASN510
BFAO1531
BUNX2501

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNX B2501
ChainResidue
BVAL464
BHIS466
BASN510
BFAO1531
BDMS1533
BUNX2500

Functional Information from PROSITE/UniProt
site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GAidTPkLLmlSGIG
ChainResidueDetails
AGLY270-GLY284

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:E4QP00
ChainResidueDetails
AHIS466
BHIS466

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
ASER23
BSER23
BGLU44
BTRP71
BALA90
BCYS96
BALA232
BTYR465
BALA500
BASN510
AGLU44
ATRP71
AALA90
ACYS96
AALA232
ATYR465
AALA500
AASN510

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Tele-8alpha-FAD histidine
ChainResidueDetails
AHIS99
BHIS99

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kdg
ChainResidueDetails
AHIS466
AASN510

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kdg
ChainResidueDetails
BHIS466
BASN510

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PDB entries from 2024-10-09

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