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2A1Y

Crystal Structure of GuaC-GMP complex from Bacillus anthracis at 2.26 A Resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003920molecular_functionGMP reductase activity
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A1902560cellular_componentGMP reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 5GP A 1344
ChainResidue
AALA43
AARG211
AMET228
AGLY230
ASER231
ATYR254
AGLY256
ASER257
AHOH1345
AHOH1366
AHOH1444
AMET45
AHOH1447
AHOH1473
AHOH1480
AGLY172
ALYS173
ACYS175
ATHR177
AASP207
AGLY208
AGLY209

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. TKVGIGpGKVCiT
ChainResidueDetails
ATHR165-THR177

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIAdGGIrTngdVakSIrFGA
ChainResidueDetails
AILE204-ALA224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_01511
ChainResidueDetails
ACYS175

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01511
ChainResidueDetails
AILE204

219869

PDB entries from 2024-05-15

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