Structure of PDB 1nhc Chain F

Receptor sequence
>1nhcF (length=336) Species: 5061 (Aspergillus niger) [Search protein sequence]
STCTFTSASEASESISSCSDVVLSSIEVPAGETLDLSDAADGSTITFEGT
TSFGYKEWKGPLIRFGGKDLTVTMADGAVIDGDGSRWWDSKGTNGGKTKP
KFMYIHDVEDSTFKGINIKNTPVQAISVQATNVHLNDFTIDNSDGDDNGG
HNTDGFDISESTGVYISGATVKNQDDCIAINSGESISFTGGTCSGGHGLS
IGSVGGRDDNTVKNVTISDSTVSNSANGVRIKTIYKETGDVSEITYSNIQ
LSGITDYGIVIEQDYENGSPTGTPSTGIPITDVTVDGVTGTLEDDATQVY
ILCGDGSCSDWTWSGVDLSGGKTSDKCENVPSGASC
3D structure
PDB1nhc Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger.
ChainF
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) D186 D207 D208 H229 R262 K264
Catalytic site (residue number reindexed from 1) D154 D175 D176 H197 R230 K232
Enzyme Commision number 3.2.1.15: endo-polygalacturonase.
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 MAN F F37 E42 S46 F5 E10 S14
BS02 GOL F R96 H138 R64 H106
Gene Ontology
Molecular Function
GO:0004650 polygalacturonase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045490 pectin catabolic process
GO:0071555 cell wall organization
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1nhc, PDBe:1nhc, PDBj:1nhc
PDBsum1nhc
PubMed14623112
UniProtP26213|PGLR1_ASPNG Endopolygalacturonase I (Gene Name=pgaI)

[Back to BioLiP]