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1ME8

Inosine Monophosphate Dehydrogenase (IMPDH) From Tritrichomonas Foetus with RVP bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 900
ChainResidue
AGLY20
ASER22
AASP264
APHE266
AASN460

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 901
ChainResidue
AGLY486
AGLY487
AHIS489
AGLY314
AGLY316
ACSO319
AGLU485

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE RVP A 602
ChainResidue
AALA57
AGLY316
ASER317
AILE318
ACSO319
AASP358
AGLY359
AGLY360
AMET379
ALEU380
AGLY381
AARG382
ATYR405
AGLY407
AGLU408
AGLY409
AGLU431
AGLY432
AHOH914
AHOH928
AHOH937
AHOH975
AHOH1047

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKIGIGgGSICiT
ChainResidueDetails
AILE309-THR321

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:12235158, ECO:0000269|PubMed:12549902
ChainResidueDetails
ACSO319

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AARG418

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: in other chain => ECO:0000269|PubMed:12549902
ChainResidueDetails
AGLY20
ASER22
AGLY314
AGLY316
ACSO319
AASN460

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AASP261
AGLY312
ASER317
AASP358
AGLY381
ATYR405
AGLU431

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12549902
ChainResidueDetails
AASP264
APHE266
AGLU485
AGLY486
AGLY487

223166

PDB entries from 2024-07-31

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