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4MHN

Crystal structure of a glutaminyl cyclase from Ixodes scapularis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008270molecular_functionzinc ion binding
A0016603molecular_functionglutaminyl-peptide cyclotransferase activity
A0016746molecular_functionacyltransferase activity
A0017186biological_processpeptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AASP144
AGLU184
AHIS322
AHOH827

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q16769
ChainResidueDetails
AGLU183

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:24598748
ChainResidueDetails
AASP238

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:24598748, ECO:0007744|PDB:4MHN, ECO:0007744|PDB:4MHY
ChainResidueDetails
AHIS322
AGLU184
AASP144

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN57
AASN288

219869

PDB entries from 2024-05-15

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