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

4DQW

Crystal Structure Analysis of PA3770

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005524molecular_functionATP binding
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005524molecular_functionATP binding
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP A 501
ChainResidue
ATHR134
ALYS181
AMN502
AATP503
AMN504
BARG136
BARG178
BGLU180
BATP501
BMN502
BHOH654
AGLY135
BHOH700
AARG136
AASP137
ATHR153
ALEU158
AVAL159
AILE179
AGLU180

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 502
ChainResidue
AGLU180
AATP501
AATP503
AMN504

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP A 503
ChainResidue
AVAL94
APRO97
AVAL98
APHE118
AGLY120
AGLU180
ALYS181
ALEU194
ATHR196
AARG198
AASP199
AATP501
AMN502
AMN504

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 504
ChainResidue
AGLU180
AATP501
AMN502
AATP503
BATP501
BHOH700

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 505
ChainResidue
AGLY338
AGLY339
AGLY360
ASER361
AHOH615
AHOH697

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 506
ChainResidue
AHIS89
AALA203
ATYR206

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP B 501
ChainResidue
AARG136
AARG178
AGLU180
AATP501
AMN504
BILE132
BTHR134
BARG136
BASP137
BTHR153
BLYS157
BLEU158
BVAL159
BILE179
BGLU180
BLYS181
BMN502
BATP503
BMN504
BHOH700

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 502
ChainResidue
AATP501
BGLU180
BATP501
BATP503
BMN504
BHOH654
BHOH700

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP B 503
ChainResidue
BVAL94
BPRO97
BVAL98
BPHE118
BSER119
BGLY120
BGLU180
BLYS181
BLEU194
BTHR196
BARG198
BASP199
BATP501
BMN502
BMN504
BHOH654

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 504
ChainResidue
BATP503
BGLU180
BATP501
BMN502

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL294-THR306

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon