Structure of PDB 4fns Chain D

Receptor sequence
>4fnsD (length=718) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
KQFHLRAGKASYVMQLFRSGYLAHVYWGKAVRDVRGARAFPRLDRAFSPN
PDPSDRTFSLDTLLQEYPAYGNTDFRAPAYQVQLENGSTVTDLRYKTHRI
YKGKPRLNGLPATYVEHEQEAETLEIVLGDALIGLEVTLQYTAYEKWNVI
TRSARFENKGGERLKLLRALSMSVDFPTADYDWIHLPGAWGRERWIERRP
LVTGVQAAESRRGASSHQQNPFIALVAKNADEHQGEVYGFSFVYSGNFLA
QIEVDQFGTARVSMGINPFDFTWLLQPGESFQTPEVVMVYSDQGLNGMSQ
TYHELYRTRLARGAFRDRERPILINNWEATYFDFNEEKIVNIARTEAELG
IELVVLDDGWFGERDDDRRSLGDWIVNRRKLPNGLDGLAKQVNELGLQFG
LWVEPEMVSPNSELYRKHPDWCLHVPNRPRSEGRNQLVLDYSREDVCDYI
IETISNVLASAPITYVKWDMNRHMTEIGSSALPPERQRETAHRYMLGLYR
VMDEITSRLPHILFESCSGGGGRFDPGMLYYMPQTWTSDNTDAVSRLKIQ
YGTSLVYPISAMGAHVSAVPNHQVGRVASLKTRGHVAMSGNFGYELDITK
LTETEKQMMKQQVAFYKDVRRLVQFGTFYRLLSPFEGNEAAWMFVSADRS
EALVAYFRVLAEANAPLSYLRLKGLDSNQDYEIEGLGVYGGDELVYAGVA
LPYRSSDFISMMWRLKAV
3D structure
PDB4fns The molecular mechanism of the thermostable alpha-galactosidases AgaA and AgaB explained by X-ray crystallography and mutational studies
ChainD
Resolution2.6 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.2.1.22: alpha-galactosidase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 DGJ D W336 D366 D367 W411 R443 K476 D478 N480 C526 G528 D548 W327 D357 D358 W402 R434 K467 D469 N471 C517 G519 D539 PDBbind-CN: -logKd/Ki=6.70,Ki=0.2uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004557 alpha-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
GO:0033531 stachyose metabolic process
GO:0034484 raffinose catabolic process
GO:0051289 protein homotetramerization

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4fns, PDBe:4fns, PDBj:4fns
PDBsum4fns
PubMed23012371
UniProtQ9ALJ4|AGAA_GEOSE Alpha-galactosidase AgaA (Gene Name=agaA)

[Back to BioLiP]