Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6RPC

GOLGI ALPHA-MANNOSIDASE II

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 Residues7
Detailsbinding site for residue EDO A 1101
ChainResidue
AARG176
AASN177
AMET433
AVAL436
AHOH1240
AHOH1501
AHOH1609

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 1102
ChainResidue
AHIS273
AHOH1309
AHOH1369
AHOH1505
ALYS63
ATYR267

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 1103
ChainResidue
ALEU568
AASP570
AARG617
AGLU753
AHOH1243

site_idAC4
Number of Residues1
Detailsbinding site for residue EDO A 1104
ChainResidue
AGLU936

site_idAC5
Number of Residues9
Detailsbinding site for residue SIN A 1105
ChainResidue
ASER534
AARG540
ATYR572
AARG617
AARG777
AHOH1266
AHOH1267
AHOH1588
AHOH1712

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 1106
ChainResidue
AVAL43
AGLU236
AGLN242
AHOH1237
AHOH1268

site_idAC7
Number of Residues10
Detailsbinding site for residue EDO A 1107
ChainResidue
AASP204
APHE206
AARG228
ATYR727
AARG876
AHOH1201
AHOH1250
AHOH1475
AHOH1490
AHOH1610

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO A 1108
ChainResidue
ATRP598
AGLN766
ALEU779
AHOH1260
AHOH1378

site_idAC9
Number of Residues5
Detailsbinding site for residue ZN A 1109
ChainResidue
AHIS90
AASP92
AASP204
AHIS471
AHOH1352

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

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon