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1EMS

CRYSTAL STRUCTURE OF THE C. ELEGANS NITFHIT PROTEIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0006139biological_processnucleobase-containing compound metabolic process
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0043605biological_processamide catabolic process
A0047710molecular_functionbis(5'-adenosyl)-triphosphatase activity
A0110050molecular_functiondeaminated glutathione amidase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0006139biological_processnucleobase-containing compound metabolic process
B0016787molecular_functionhydrolase activity
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0043605biological_processamide catabolic process
B0047710molecular_functionbis(5'-adenosyl)-triphosphatase activity
B0110050molecular_functiondeaminated glutathione amidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EMC A 451
ChainResidue
AGLU54
ALYS127
AGLU143
ACYS169
AALA194

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EMC B 452
ChainResidue
BALA194
BGLU54
BLYS127
BGLU143
BCYS169

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EMC A 453
ChainResidue
ACYS55
AGLY96
AHIS98
AASN110
ASER147

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EMC A 454
ChainResidue
ACYS75
APHE304
AVAL388

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EMC B 455
ChainResidue
BCYS55
BGLY96
BLEU97
BHIS98
BASN110

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 456
ChainResidue
ATYR218
AHOH531
BSER252

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 457
ChainResidue
ASER167
ASER178
AASN181
ALEU189
AHOH561

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 458
ChainResidue
BMET71
BCYS75
BGLU76
BTYR77

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 459
ChainResidue
ACYS377
AGLN379
AHIS394

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 502
ChainResidue
AGLU253
BMET273

Functional Information from PROSITE/UniProt
site_idPS00892
Number of Residues19
DetailsHIT_1 HIT domain signature. QdgkdAgQtVpHVHIHILP
ChainResidueDetails
AGLN379-PRO397

site_idPS01227
Number of Residues21
DetailsUPF0012 Uncharacterized protein family UPF0012 signature. GlsICYDVrFPelslwnrkrG
ChainResidueDetails
AGLY165-GLY185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues500
DetailsDomain: {"description":"CN hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00054","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"Histidine triad motif"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PubMed","id":"9671749","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"UniProtKB","id":"P49789","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00054","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 5fit
ChainResidueDetails
AHIS392
AGLN379
AHIS390

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 5fit
ChainResidueDetails
BHIS392
BGLN379
BHIS390

245663

PDB entries from 2025-12-03

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