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

4ML8

Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009690biological_processcytokinin metabolic process
A0016491molecular_functionoxidoreductase activity
A0019139molecular_functioncytokinin dehydrogenase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
B0003824molecular_functioncatalytic activity
B0009690biological_processcytokinin metabolic process
B0016491molecular_functionoxidoreductase activity
B0019139molecular_functioncytokinin dehydrogenase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0071949molecular_functionFAD binding
C0003824molecular_functioncatalytic activity
C0009690biological_processcytokinin metabolic process
C0016491molecular_functionoxidoreductase activity
C0019139molecular_functioncytokinin dehydrogenase activity
C0050660molecular_functionflavin adenine dinucleotide binding
C0071949molecular_functionFAD binding
D0003824molecular_functioncatalytic activity
D0009690biological_processcytokinin metabolic process
D0016491molecular_functionoxidoreductase activity
D0019139molecular_functioncytokinin dehydrogenase activity
D0050660molecular_functionflavin adenine dinucleotide binding
D0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD A 601
ChainResidue
APHE55
ATHR157
AASP158
ATYR159
ALEU162
ATHR163
AGLY165
AGLY166
ATHR167
ASER169
AASN170
AALA95
AGLY172
AVAL173
AGLY219
AGLY222
AILE223
AILE224
ATRP373
ATYR469
AGLN507
AGLY97
AHIS98
AGLY99
AHIS100
ASER101
AGLN105
ASER106

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG A 602
ChainResidue
AARG53
AARG96
AHIS98
AGLY99
AHIS100
ATYR159
ATRP367
AGLU368
AHOH727

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD B 601
ChainResidue
BPHE55
BALA95
BGLY97
BHIS98
BGLY99
BHIS100
BSER101
BGLN105
BSER106
BTHR157
BASP158
BTYR159
BTHR163
BGLY166
BTHR167
BSER169
BASN170
BGLY172
BVAL173
BGLY219
BGLY222
BILE223
BILE224
BTRP373
BTYR469
BGLN507
BHOH721

site_idAC4
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD C 601
ChainResidue
CPHE55
CALA95
CGLY97
CHIS98
CGLY99
CHIS100
CSER101
CGLN105
CSER106
CTHR157
CASP158
CTYR159
CLEU162
CTHR163
CGLY165
CGLY166
CTHR167
CSER169
CASN170
CGLY172
CVAL173
CGLY219
CGLY222
CILE223
CILE224
CTRP373
CTYR469
CGLN507
CHOH719

site_idAC5
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD D 601
ChainResidue
DSER101
DGLN105
DSER106
DTHR157
DASP158
DTYR159
DLEU162
DTHR163
DGLY166
DTHR167
DSER169
DASN170
DGLY172
DVAL173
DGLY219
DGLY222
DILE223
DILE224
DTRP373
DTYR469
DGLN507
DPHE55
DALA95
DGLY97
DHIS98
DGLY99
DHIS100

Functional Information from PROSITE/UniProt
site_idPS00862
Number of Residues36
DetailsOX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PaavlhpgSvsDIaatVrhvfslgegsp.LtvaARGH
ChainResidueDetails
APRO63-HIS98

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon