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5AJN

Crystal structure of the inactive form of GalNAc-T2 in complex with the glycopeptide MUC5AC-Cys13

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0004653molecular_functionpolypeptide N-acetylgalactosaminyltransferase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005795cellular_componentGolgi stack
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0016020cellular_componentmembrane
A0016266biological_processO-glycan processing
A0016757molecular_functionglycosyltransferase activity
A0018242biological_processprotein O-linked glycosylation via serine
A0018243biological_processprotein O-linked glycosylation via threonine
A0030145molecular_functionmanganese ion binding
A0030246molecular_functioncarbohydrate binding
A0032580cellular_componentGolgi cisterna membrane
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0051604biological_processprotein maturation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc) threonine => ECO:0000269|PubMed:25939779, ECO:0007744|PDB:5AJO
ChainResidueDetails
PTHR3

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc) threonine => ECO:0000269|PubMed:25939779, ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP
ChainResidueDetails
PCYS13

site_idSWS_FT_FI3
Number of Residues546
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
ASER25-GLN571

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9
ChainResidueDetails
ATHR143
AASP176
AARG201
ASER225
ATRP331
AARG362
AHIS365

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11, ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9
ChainResidueDetails
AASP224
AHIS226
AHIS359

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11, ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9, ECO:0007744|PDB:5NDF, ECO:0007744|PDB:6EGS
ChainResidueDetails
ATYR367

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Not glycosylated
ChainResidueDetails
AASP516

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER536

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: O-linked (Xyl...) (chondroitin sulfate) serine => ECO:0000269|PubMed:37453717
ChainResidueDetails
ASER29

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PDB entries from 2024-07-24

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