Structure of PDB 1h12 Chain A

Receptor sequence
>1h12A (length=404) Species: 228 (Pseudoalteromonas haloplanktis) [Search protein sequence]
AFNNNPSSVGAYSSGTYRNLAQEMGKTNIQQKVNSTFDNMFGYNNTQQLY
YPYTENGVYKAHYIKAINPDEGDDIRTEGQSWGMTAAVMLNKQEEFDNLW
RFAKAYQKNPDNHPDAKKQGVYAWKLKLNQNGFVYKVDEGPAPDGEEYFA
FALLNASARWGNSGEFNYYNDAITMLNTIKNKLMENQIIRFSPYIDNLTD
PSYHIPAFYDYFANNVTNQADKNYWRQVATKSRTLLKNHFTKVSGSPHWN
LPTFLSRLDGSPVIGYIFNGQANPGQWYEFDAWRVIMNVGLDAHLMGAQA
WHKSAVNKALGFLSYAKTNNSKNCYEQVYSYGGAQNRGCAGEGQKAANAV
ALLASTNAGQANEFFNEFWSLSQPTGDYRYYNGSLYMLAMLHVSGNFKFY
NNTF
3D structure
PDB1h12 The Structure of a Cold-Adapted Family 8 Xylanase at 1.3 A Resolution: Structural Adaptations to Cold and Investigation of the Active Site
ChainA
Resolution1.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.4: cellulase.
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 XYP A Q327 Y378 N382 Q327 Y378 N382
BS02 XYS A Q327 Y378 N382 Q327 Y378 N382
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1h12, PDBe:1h12, PDBj:1h12
PDBsum1h12
PubMed12475991
UniProtQ8RJN8

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