3HG2: Alpha-galactosidase A

Human alpha-galactosidase catalytic mechanism 1. Empty active site. Determined by X-ray diffraction at 2.3 Å resolution. Released 24 Nov 2009.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
2
Atoms
6,765
Mol. weight
93.64 kDa
Ligands
NAG, GAL
Released
24 Nov 2009

Explore 3HG2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HG2 contains 34 α-helices and 46 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 23 β-strands

ElementResiduesLengthSheet
β-strand42-4541
α-helix47-504
α-helix66-7813
α-helix81-844
β-strand88-9031
β-strand9612
β-strand10812
α-helix117-12610
β-strand130-13671
β-strand14013
β-strand14613
α-helix1471
α-helix152-16211
β-strand166-17051
α-helix177-19418
β-strand199-20241
α-helix204-2085
α-helix216-2227
β-strand225-22731
α-helix230-2323
α-helix236-24813
α-helix250-2534
β-strand25814
β-strand26114
β-strand262-26431
β-strand26811
α-helix277-28913
β-strand294-29631
α-helix305-3117
α-helix314-3207
β-strand329-33465
β-strand337-34375
β-strand348-35585
β-strand363-36866
α-helix369-3713
α-helix373-3753
β-strand381-38885
β-strand392-39875
β-strand402-40766
β-strand412-41985
Chain B: 17 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand42-4547
α-helix47-504
α-helix66-7813
α-helix81-844
β-strand88-9037
β-strand9618
β-strand10818
α-helix116-12611
β-strand130-13677
β-strand14019
β-strand14619
α-helix1471
α-helix152-16211
β-strand166-17057
α-helix177-19216
β-strand199-20247
α-helix204-2085
α-helix216-2227
β-strand225-22737
α-helix230-2323
α-helix236-24813
α-helix250-2534
β-strand258110
β-strand261110
β-strand262-26437
β-strand26817
α-helix277-28913
β-strand294-29637
α-helix305-3117
α-helix314-3207
β-strand329-334611
β-strand337-343711
α-helix345-3473
β-strand349-355711
β-strand363-368612
α-helix369-3757
β-strand381-388811
β-strand392-398711
β-strand402-407612
β-strand412-420911

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-galactosidase AA, Bprotein398Homo sapiensP06280 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3HG2_1 Alpha-galactosidase A (chains A, B)
LDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCI
DDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGY
YDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPF
QKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIG
NFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQL
RQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVK
RKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O63
GALbeta-D-galactopyranoseC6 H12 O61

Water and common crystallization additives (SO4, ACY) are not listed.

Primary citation

Catalytic mechanism of human alpha-galactosidase. Guce, A.I., Clark, N.E., Salgado, E.N. et al. J Biol Chem (2010) 285:3625-3632. DOI 10.1074/jbc.M109.060145 · PubMed

Other PDB entries of the same protein (UniProt P06280 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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