Structure of PDB 6d5d Chain A

Receptor sequence
>6d5dA (length=627) Species: 1387557 (Caldicellulosiruptor danielii) [Search protein sequence]
LGEYGQRFMWLWNKIHDPANGYFNQDGIPYHSVETLICEAPDYGHLTTSE
AFSYYVWLEAVYGKLTGDWSKFKTAWDTLEKYMIPSAEDQPMRSYDPNKP
ATYAGEWETPDKYPSPLEFNVPVGKDPLHNELVSTYGSTLMYGMHWLMDV
DNWYGYGKRGDGVSRASFINTFQRGPEESVWETVPHPSWEEFKWGGPNGF
LDLFIKDQNYSKQWRYTNAPDADARAIQATYWAKEWAKEQGKFNEISSYV
AKAAKMGDYLRYAMFDKYFKPLGCQDKNAAGGTGYDSAHYLLSWYYAWGG
ALDGAWSWKIGCSHAHFGYQNPMAAWALANDSDMKPKSPNGASDWAKSLK
RQIEFYRWLQSAEGAIAGGATNSWNGRYEKYPAGTATFYGMAYEPNPVYR
DPGSNTWFGFQAWSMQRVAEYYYVTGDKDAGALLEKWVSWIKSVVKLNSD
GTFAIPSTLDWSGQPDTWNGTYTGNPNLHVKVVDYGTDLGITASLANALL
YYSAATKKYGVFDEEAKNLAKELLDRMWKLYRDEKGLSAPEKRADYKRFF
EQEVYIPAGWTGKMPNGDVIKSGVKFIDIRSKYKQDPDWPKLEAAYKSGQ
VPEFRYHRFWAQCDIAIANATYEILFG
3D structure
PDB6d5d Novel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.-
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 D504 R624 W626 D488 R608 W610
BS02 BGC A H47 E55 E66 W423 W429 H31 E39 E50 W407 W413
BS03 BGC A A117 Q229 W324 A101 Q213 W308
BS04 BGC A A117 T118 A101 T102
BS05 CA A E193 E198 D417 E177 E182 D401
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6d5d, PDBe:6d5d, PDBj:6d5d
PDBsum6d5d
PubMed
UniProtA0A4V8GZQ9

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