Structure of PDB 1clc Chain A

Receptor sequence
>1clcA (length=541) Species: 1515 (Acetivibrio thermocellus) [Search protein sequence]
IETKVSAAKITENYQFDSRIRLNSIGFIPNHSKKATIAANCSTFYVVKED
GTIVYTGTATSMFDNDTKETVYIADFSSVNEEGTYYLAVPGVGKSVNFKI
AMNVYEDAFKTAMLGMYLLRCGTSVSATYNGIHYSHGPCHTNDAYLDYIN
GQHTKKDSTKGWHDAGDYNKYVVNAGITVGSMFLAWEHFKDQLEPVALEI
PEKNNSIPDFLDELKYEIDWILTMQYPDGSGRVAHKVSTRNFGGFIMPEN
EHDERFFVPWSSAATADFVAMTAMAARIFRPYDPQYAEKCINAAKVSYEF
LKNNPANVFANQSGFSTGEYATVSDADDRLWAAAEMWETLGDEEYLRDFE
NRAAQFSKKIEADFDWDNVANLGMFTYLLSERPGKNPALVQSIKDSLLST
ADSIVRTSQNHGYGRTLGTTYYWGCNGTVVRQTMILQVANKISPNNDYVN
AALDAISHVFGRNYYNRSYVTGLGINPPMNPHDRRSGADGIWEPWPGYLV
GGGWPGPKDWVDIQDSYQTNEIAINWNAALIYALAGFVNYN
3D structure
PDB1clc Three-Dimensional Structure of a Thermostable Bacterial Cellulase
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D198 D201 Y354 E555
Catalytic site (residue number reindexed from 1) D164 D167 Y320 E521
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 CA A E236 K237 N239 I241 D243 D246 E202 K203 N205 I207 D209 D212
BS02 CA A T356 S358 D361 D362 D401 T322 S324 D327 D328 D367
BS03 CA A S520 D523 I525 S486 D489 I491
BS04 ZN A C155 C173 H174 H197 C121 C139 H140 H163
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1clc, PDBe:1clc, PDBj:1clc
PDBsum1clc
PubMed
UniProtP0C2S4|GUND_ACETH Endoglucanase D (Fragment) (Gene Name=celD)

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