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3PBB

Crystal structure of human secretory glutaminyl cyclase in complex with PBD150

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
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
A0035580cellular_componentspecific granule lumen
A0036211biological_processprotein modification process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0008270molecular_functionzinc ion binding
B0016603molecular_functionglutaminyl-peptide cyclotransferase activity
B0016746molecular_functionacyltransferase activity
B0017186biological_processpeptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
B0035580cellular_componentspecific granule lumen
B0036211biological_processprotein modification process
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PBD A 380
ChainResidue
ATYR115
ASER323
APHE325
AHIS330
AZN391
AHOH632
ATYR145
AASP159
AGLU201
AGLU202
ATRP207
AASP248
ATYR299
AGLN304

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 391
ChainResidue
AASP159
AGLU202
AHIS330
APBD380

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PBD B 381
ChainResidue
BTYR115
BARG118
BTYR145
BASP159
BGLU201
BGLU202
BTRP207
BASP248
BGLN304
BSER323
BPHE325
BTRP329
BHIS330
BZN392
BHOH602

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 392
ChainResidue
BASP159
BGLU202
BHIS330
BPBD381

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:18072935
ChainResidueDetails
AGLU201
AASP248
BGLU201
BASP248

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935, ECO:0000269|PubMed:21288892, ECO:0000269|PubMed:21671571, ECO:0007744|PDB:2AFM, ECO:0007744|PDB:2AFO, ECO:0007744|PDB:2AFS, ECO:0007744|PDB:2AFU, ECO:0007744|PDB:2AFW, ECO:0007744|PDB:2AFX, ECO:0007744|PDB:2AFZ, ECO:0007744|PDB:2ZED, ECO:0007744|PDB:2ZEE, ECO:0007744|PDB:2ZEF, ECO:0007744|PDB:2ZEG, ECO:0007744|PDB:2ZEH, ECO:0007744|PDB:2ZEL, ECO:0007744|PDB:2ZEM, ECO:0007744|PDB:2ZEN, ECO:0007744|PDB:2ZEO, ECO:0007744|PDB:2ZEP, ECO:0007744|PDB:3PBB, ECO:0007744|PDB:3PBE, ECO:0007744|PDB:3SI0, ECO:0007744|PDB:4YU9, ECO:0007744|PDB:4YWY
ChainResidueDetails
AASP159
AGLU202
AHIS330
BASP159
BGLU202
BHIS330

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21671571
ChainResidueDetails
AASN49
BASN49

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN296
BASN296

219869

PDB entries from 2024-05-15

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