Structure of PDB 1uu5 Chain A

Receptor sequence
>1uu5A (length=224) [Search protein sequence]
EIRSLCELYGYWSGNGYELLNNLWGKDTATSGWQCTYLDGTNNGGIQWST
AWEWQGAPDNVKSYPYVGKQIQRGRKISDINSMRTSVSWTYDRTDIRANV
AYDVFTARDPDHPNWGGDYELMIWLARYGGIYPIGTFHSQVNLAGRTWDL
WTGYNGNMRVYSFLPPSGDIRDFSCDIKDFFNYLERNHGYPAREQNLIVY
QVGTECFTGGPARFTCRDFRADLW
3D structure
PDB1uu5 Crystal Complex Structures Reveal How Substrate is Bound in the -4 to the +2 Binding Sites of Humicola Grisea Cel12A
ChainA
Resolution1.67 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E120 E205
Catalytic site (residue number reindexed from 1) E120 E205
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 BGC A W24 Y64 E120 N155 E205 W24 Y64 E120 N155 E205
BS02 BGC A W24 W115 W24 W115
BS03 BGC A Y9 L20 Y66 N114 Y9 L20 Y66 N114
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:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1uu5, PDBe:1uu5, PDBj:1uu5
PDBsum1uu5
PubMed15364577
UniProtQ8NJY3

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