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5ZBL

Crystal structure of type-I LOG from Corynebacterium glutamicum in complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005829cellular_componentcytosol
A0009691biological_processcytokinin biosynthetic process
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0102682molecular_functioncytokinin riboside 5'-monophosphate phosphoribohydrolase activity
B0000166molecular_functionnucleotide binding
B0005829cellular_componentcytosol
B0009691biological_processcytokinin biosynthetic process
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0102682molecular_functioncytokinin riboside 5'-monophosphate phosphoribohydrolase activity
C0000166molecular_functionnucleotide binding
C0005829cellular_componentcytosol
C0009691biological_processcytokinin biosynthetic process
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0102682molecular_functioncytokinin riboside 5'-monophosphate phosphoribohydrolase activity
D0000166molecular_functionnucleotide binding
D0005829cellular_componentcytosol
D0009691biological_processcytokinin biosynthetic process
D0016787molecular_functionhydrolase activity
D0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
D0102682molecular_functioncytokinin riboside 5'-monophosphate phosphoribohydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 301
ChainResidue
AASP143
AGLN149
AVAL174
AGLU175
BSER24
BSER25

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 302
ChainResidue
BHIS97
BLYS100
BGLU125
AHIS97
ALYS100
AGLU125

site_idAC3
Number of Residues8
Detailsbinding site for residue PO4 A 303
ChainResidue
AGLY18
ASER19
AGLY116
AALA117
AGLY118
ATHR119
AHOH403
BGLN131

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 304
ChainResidue
AASP95
AMET96
BHIS97

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO B 301
ChainResidue
AGLU75
AILE92
APRO94
BHIS84
BGLU85
BLYS86
BLEU87

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO B 302
ChainResidue
AHIS84
AGLU85
ALYS86
ALEU87
BILE92
BVAL93
BPRO94

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL B 303
ChainResidue
BVAL15
BPHE16
BTHR17
BTYR47
BGLY48
BMET55
BARG99
BGLU122
BHOH401

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 304
ChainResidue
AGLY66
BLEU63
BGLU64
BGLY66

site_idAC9
Number of Residues8
Detailsbinding site for residue PO4 B 305
ChainResidue
BGLY18
BSER19
BGLY116
BALA117
BGLY118
BTHR119
BHOH401
BHOH406

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 B 306
ChainResidue
BGLN32
BLYS36
BALA61
BGLU64
BSER65

site_idAD2
Number of Residues4
Detailsbinding site for residue SO4 B 307
ChainResidue
AHIS97
BTHR74
BASP95
BMET96

site_idAD3
Number of Residues18
Detailsbinding site for residue AMP C 301
ChainResidue
CTHR17
CGLY18
CSER19
CMET55
CARG99
CLYS100
CGLY116
CALA117
CGLY118
CTHR119
CGLU121
CGLU122
CHOH407
CHOH409
DGLU125
DTHR128
DTRP129
DHOH406

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL C 302
ChainResidue
CHIS97
CLYS100
CGLU125
CHOH405
DHIS97
DLYS100
DGLU125

site_idAD5
Number of Residues14
Detailsbinding site for residue AMP D 301
ChainResidue
DALA117
DGLY118
DTHR119
DGLU121
DGLU122
DHOH402
DHOH403
CTHR128
DTHR17
DSER19
DMET55
DARG99
DLYS100
DGLY116

site_idAD6
Number of Residues5
Detailsbinding site for residue GOL D 302
ChainResidue
DLEU21
DLYS51
DVAL52
DGLY53
DILE57

site_idAD7
Number of Residues2
Detailsbinding site for residue SO4 D 303
ChainResidue
DASP177
DHIS179

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PDB entries from 2024-07-24

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