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6RQZ

GOLGI ALPHA-MANNOSIDASE II complex with Manno-epi-cyclophellitol aziridine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0003824molecular_functioncatalytic activity
A0004559molecular_functionalpha-mannosidase activity
A0004572molecular_functionmannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005795cellular_componentGolgi stack
A0005975biological_processcarbohydrate metabolic process
A0006013biological_processmannose metabolic process
A0006486biological_processobsolete protein glycosylation
A0006487biological_processprotein N-linked glycosylation
A0006491biological_processN-glycan processing
A0015923molecular_functionmannosidase activity
A0016063biological_processrhodopsin biosynthetic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0035010biological_processencapsulation of foreign target
A0046872molecular_functionmetal ion binding
A1904381biological_processGolgi apparatus N-glycan mannose trimming
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 1201
ChainResidue
AARG176
AASN177
AMET433
AVAL436
AHOH1346
AHOH1522
AHOH1688

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 1202
ChainResidue
AHIS273
AHOH1536
AHOH1599
AHOH1617
ALYS63
ATYR267

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 1203
ChainResidue
ALEU568
AASP570
AARG617
AGLU753
AHOH1511

site_idAC4
Number of Residues1
Detailsbinding site for residue EDO A 1204
ChainResidue
AGLU936

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 1205
ChainResidue
AARG228
ATYR267
AASP409
AKGH1210
AHOH1502

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO A 1206
ChainResidue
AASP340
AASP341
AARG343
AHOH1503

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 1207
ChainResidue
AARG457
AALA496
AHOH1587

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO A 1208
ChainResidue
ASER552
ALYS553
AHIS554
APHE934
AASN937
AHOH1552

site_idAC9
Number of Residues9
Detailsbinding site for residue SIN A 1209
ChainResidue
ASER534
AARG540
ATYR572
AARG617
AARG777
AHOH1355
AHOH1385
AHOH1464
AHOH1861

site_idAD1
Number of Residues17
Detailsbinding site for residue KGH A 1210
ChainResidue
AHIS90
AASP92
ATRP95
AASP204
APHE206
AARG228
ATYR269
AASP341
ATRP415
AHIS471
AASP472
ATYR727
AARG876
AEDO1205
AZN1211
AHOH1351
AHOH1687

site_idAD2
Number of Residues5
Detailsbinding site for residue ZN A 1211
ChainResidue
AHIS90
AASP92
AASP204
AHIS471
AKGH1210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 793
ChainResidueDetails
AHIS90metal ligand
AASP92metal ligand
AASP204covalently attached, metal ligand, nucleofuge, nucleophile
AASP341activator, increase nucleophilicity, proton acceptor, proton donor
AHIS471metal ligand

247947

PDB entries from 2026-01-21

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