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6RRY

GOLGI ALPHA-MANNOSIDASE II in complex with (2S,3R)-2-(Hydroxymethyl)-1,2,3,6-tetrahydro-3-pyridinol

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_processprotein glycosylation
A0006491biological_processN-glycan processing
A0015923molecular_functionmannosidase activity
A0016020cellular_componentmembrane
A0016063biological_processrhodopsin biosynthetic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0035010biological_processencapsulation of foreign target
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 1101
ChainResidue
AARG176
AASN177
AMET433
AVAL436
AHOH1254
AHOH1297

site_idAC2
Number of Residues9
Detailsbinding site for residue KGE A 1102
ChainResidue
APHE206
AARG228
AHIS471
AASP472
ATYR727
AZN1106
AASP92
ATRP95
AASP204

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 1103
ChainResidue
ALYS63
AHIS273
AHOH1228
AHOH1361
AHOH1579

site_idAC4
Number of Residues9
Detailsbinding site for residue SIN A 1104
ChainResidue
ASER534
AARG540
ATYR572
AARG617
AGLN766
AARG777
AHOH1347
AHOH1479
AHOH1510

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 1105
ChainResidue
ALEU568
AASP570
AARG617
AGLU753
AHOH1421

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN A 1106
ChainResidue
AHIS90
AASP92
AASP204
AHIS471
AKGE1102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP204

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS90
AASP92
AASP204
AHIS471

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

221716

PDB entries from 2024-06-26

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