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1Y43

crystal structure of aspergilloglutamic peptidase from Aspergillus niger

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070007molecular_functionglutamic-type endopeptidase activity
B0006508biological_processproteolysis
B0070007molecular_functionglutamic-type endopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
ALYS19
AALA31
BTYR5
BTYR31
BGLU68

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
ASER4
AASN6
ATRP7
BTYR48

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 203
ChainResidue
BGLU19
BASP28
BCYS30
BSER37
BPRO46
BHOH206

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 204
ChainResidue
BASP28
BPHE112
BHOH281
BHOH282

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 205
ChainResidue
BLYS64
BGLU80
BSER164
BGLY165
BHOH254

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1918059
ChainResidueDetails
BGLN1

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1s2k
ChainResidueDetails
BGLN24
BGLU110

226707

PDB entries from 2024-10-30

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