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

5MCP

Structure of IMP dehydrogenase from Ashbya gossypii bound to ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003938molecular_functionIMP dehydrogenase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006164biological_processpurine nucleotide biosynthetic process
C0006177biological_processGMP biosynthetic process
C0006183biological_processGTP biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0003938molecular_functionIMP dehydrogenase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006164biological_processpurine nucleotide biosynthetic process
D0006177biological_processGMP biosynthetic process
D0006183biological_processGTP biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0003824molecular_functioncatalytic activity
E0003938molecular_functionIMP dehydrogenase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0006164biological_processpurine nucleotide biosynthetic process
E0006177biological_processGMP biosynthetic process
E0006183biological_processGTP biosynthetic process
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0003824molecular_functioncatalytic activity
F0003938molecular_functionIMP dehydrogenase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0006164biological_processpurine nucleotide biosynthetic process
F0006177biological_processGMP biosynthetic process
F0006183biological_processGTP biosynthetic process
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0003824molecular_functioncatalytic activity
G0003938molecular_functionIMP dehydrogenase activity
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0006164biological_processpurine nucleotide biosynthetic process
G0006177biological_processGMP biosynthetic process
G0006183biological_processGTP biosynthetic process
G0016491molecular_functionoxidoreductase activity
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0003824molecular_functioncatalytic activity
H0003938molecular_functionIMP dehydrogenase activity
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0006164biological_processpurine nucleotide biosynthetic process
H0006177biological_processGMP biosynthetic process
H0006183biological_processGTP biosynthetic process
H0016491molecular_functionoxidoreductase activity
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ATP A 601
ChainResidue
ATHR165
AGLY209
ALYS210
AATP602
AHOH724
EGLN170
EMG604
EHOH703
ASER166
AARG167
AASP168
ATHR184
AASP186
AVAL187
AILE188
ALYS208

site_idAC2
Number of Residues13
Detailsbinding site for residue ATP A 602
ChainResidue
AILE121
AVAL125
APHE145
AALA146
AGLY147
ASER166
ALYS210
AMET223
ASER225
ATHR227
AASP228
AATP601
EMG604

site_idAC3
Number of Residues13
Detailsbinding site for residue ATP A 603
ChainResidue
ATHR255
AILE256
AASP257
ASER278
ASER279
APHE285
AHOH703
AHOH731
AHOH752
AHOH754
AHOH835
AHOH840
BGLN476

site_idAC4
Number of Residues17
Detailsbinding site for residue ATP B 601
ChainResidue
BILE163
BTHR165
BSER166
BARG167
BASP168
BTHR184
BASP186
BILE188
BLYS208
BGLY209
BLYS210
BATP602
BATP605
BHOH708
BHOH727
FGLN170
FMG602

site_idAC5
Number of Residues15
Detailsbinding site for residue ATP B 602
ChainResidue
BILE121
BPRO124
BVAL125
BPHE145
BALA146
BGLY147
BSER166
BLYS210
BMET223
BSER225
BTHR227
BASP228
BATP601
BHOH774
FMG602

site_idAC6
Number of Residues9
Detailsbinding site for residue ATP B 603
ChainResidue
BTHR255
BASP257
BSER278
BSER279
BPHE285
BHOH714
BHOH787
BHOH827
CGLN476

site_idAC7
Number of Residues3
Detailsbinding site for residue MG B 604
ChainResidue
BGLN170
BATP605
BATP606

site_idAC8
Number of Residues10
Detailsbinding site for residue ATP B 605
ChainResidue
BGLN170
BATP601
BMG604
BATP606
FTHR165
FSER166
FARG167
FASP168
FVAL187
FILE188

site_idAC9
Number of Residues6
Detailsbinding site for residue ATP B 606
ChainResidue
FPHE145
FGLY147
FSER166
BMG604
BATP605
FVAL125

site_idAD1
Number of Residues17
Detailsbinding site for residue ATP C 601
ChainResidue
CILE163
CTHR165
CSER166
CARG167
CASP168
CTHR184
CILE188
CLYS208
CGLY209
CLYS210
CPRO212
CATP602
CMG604
CHOH708
CHOH798
HGLN170
HHOH701

site_idAD2
Number of Residues18
Detailsbinding site for residue ATP C 602
ChainResidue
CILE121
CPRO124
CVAL125
CPHE145
CALA146
CGLY147
CSER166
CLYS210
CMET223
CSER225
CTHR227
CASP228
CATP601
CMG604
CHOH701
CHOH800
CHOH808
CHOH814

site_idAD3
Number of Residues12
Detailsbinding site for residue ATP C 603
ChainResidue
CTHR255
CILE256
CSER278
CSER279
CPHE285
CHOH714
CHOH731
CHOH781
CHOH782
CHOH787
CHOH841
DGLN476

site_idAD4
Number of Residues3
Detailsbinding site for residue MG C 604
ChainResidue
CLYS210
CATP601
CATP602

site_idAD5
Number of Residues2
Detailsbinding site for residue MG C 605
ChainResidue
HATP601
HATP602

site_idAD6
Number of Residues15
Detailsbinding site for residue ATP D 601
ChainResidue
DILE163
DTHR165
DARG167
DASP168
DTHR184
DASP186
DILE188
DLYS208
DGLY209
DLYS210
DATP602
DHOH787
GGLN170
GATP601
GMG604

site_idAD7
Number of Residues17
Detailsbinding site for residue ATP D 602
ChainResidue
DILE121
DPRO124
DVAL125
DPHE145
DALA146
DGLY147
DSER166
DLYS210
DMET223
DSER225
DTHR227
DASP228
DATP601
DHOH751
DHOH796
DHOH838
GMG604

site_idAD8
Number of Residues12
Detailsbinding site for residue ATP D 603
ChainResidue
AGLN476
DTHR255
DASP257
DSER278
DSER279
DPHE285
DHOH714
DHOH717
DHOH729
DHOH757
DHOH798
DHOH851

site_idAD9
Number of Residues2
Detailsbinding site for residue MG D 604
ChainResidue
GATP601
GATP602

site_idAE1
Number of Residues14
Detailsbinding site for residue ATP E 601
ChainResidue
ETHR165
ESER166
EARG167
EASP168
ETHR184
EASP186
EVAL187
EILE188
ELYS208
EGLY209
ELYS210
EATP602
EMG605
EHOH725

site_idAE2
Number of Residues8
Detailsbinding site for residue ATP E 602
ChainResidue
EPHE145
EALA146
EPHE148
ESER166
EMET223
ETHR227
EATP601
EMG605

site_idAE3
Number of Residues4
Detailsbinding site for residue ATP E 603
ChainResidue
ETHR255
ESER279
EPHE285
GGLN476

site_idAE4
Number of Residues4
Detailsbinding site for residue MG E 604
ChainResidue
ALYS210
AATP601
AATP602
EGLN170

site_idAE5
Number of Residues2
Detailsbinding site for residue MG E 605
ChainResidue
EATP601
EATP602

site_idAE6
Number of Residues4
Detailsbinding site for residue ATP F 601
ChainResidue
FTHR255
FILE256
FSER279
FPHE285

site_idAE7
Number of Residues3
Detailsbinding site for residue MG F 602
ChainResidue
BLYS210
BATP601
BATP602

site_idAE8
Number of Residues13
Detailsbinding site for residue ATP G 601
ChainResidue
DGLN170
DATP601
DMG604
GTHR165
GSER166
GARG167
GASP168
GTHR184
GVAL187
GILE188
GGLY209
GLYS210
GATP602

site_idAE9
Number of Residues6
Detailsbinding site for residue ATP G 602
ChainResidue
DMG604
GPHE145
GALA146
GGLY147
GSER166
GATP601

site_idAF1
Number of Residues2
Detailsbinding site for residue ATP G 603
ChainResidue
GSER278
GSER279

site_idAF2
Number of Residues3
Detailsbinding site for residue MG G 604
ChainResidue
DLYS210
DATP601
DATP602

site_idAF3
Number of Residues11
Detailsbinding site for residue ATP H 601
ChainResidue
CGLN170
CMG605
HTHR165
HSER166
HARG167
HASP168
HILE188
HGLY209
HLYS210
HATP602
HHOH701

site_idAF4
Number of Residues9
Detailsbinding site for residue ATP H 602
ChainResidue
CMG605
HVAL125
HPHE145
HALA146
HGLY147
HPHE148
HSER166
HASP228
HATP601

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRIGMGsGSICiT
ChainResidueDetails
ALEU324-THR336

225681

PDB entries from 2024-10-02

PDB statisticsPDBj update infoContact PDBjnumon