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3BXM

Structure of an inactive mutant of human glutamate carboxypeptidase II [GCPII(E424A)] in complex with N-acetyl-Asp-Glu (NAAG)

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1AGlutamate carboxypeptidase 2polymer70979801.01UniProt (Q04609)
Pfam (PF02225)
Pfam (PF04389)
Pfam (PF04253)
In PDB
Homo sapiens (human)Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, mGCP, N-acetylated-alpha-linked acidic dipeptidase I, NAALADase I, Pteroylpoly-gamma-glutamate carboxypeptidase, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Folate hydrolase 1, Prostate-specific membrane antigen, PSMA, PSM
2IN-Acetyl-Aspartyl-Glutamate (NAAG)polymer3288.31
3B, C, D2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosebranched424.43In PDB
GlyTouCan (G42666HT)
4Ealpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosebranched748.71In PDB
GlyTouCan (G81315DD)
5A2-acetamido-2-deoxy-beta-D-glucopyranosenon-polymer221.23Chemie (NAG)
6AZINC IONnon-polymer65.42Chemie (ZN)
7ACALCIUM IONnon-polymer40.11Chemie (CA)
8ACHLORIDE IONnon-polymer35.51Chemie (CL)
9waterwater18.0496Chemie (HOH)
Sequence modifications
A: 44 - 750 (UniProt: Q04609)
PDBExternal DatabaseDetails
Arg 42-expression tag
Ser 43-expression tag
Ala 424Glu 424engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains2
Total formula weight80089.2
BranchedNumber of molecules4
Total formula weight2021.9
Non-Polymers*Number of molecules7
Total formula weight870.0
All*Total formula weight82981.1
*Water molecules are not included.

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PDB entries from 2024-07-17

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