Structure of PDB 4zzw Chain A

Receptor sequence
>4zzwA (length=435) Species: 1173061 (Geotrichum candidum) [Search protein sequence]
EQIGTLTTETHPPLTWQTCTSGGSCTTNNGKVVLDANWRWLHSTSGSTNC
YTGNTWNTTLCPDDTTCAQNCALDGADYEGTYGITASGNSLRLNFVTNGS
QKNVGSRTYLMKDDTHYQTFNLLNQEFTFDVDVSGLPCGLNGALYMVPMA
ADGGVSNEPNNKAGAQYGVGYCDSQCPRDLKFIAGSANVQGWEPASNSGL
GGNGSCCAELDIWEANSISAALTPHSADTVTQTVCNGDDCGGTYSNDRYS
GTTDPDGCDFNSYRQGDTSFYGPGKTVDTNSKFTVVTQFLTDSSGNLNEI
KRFYVQNGVVIPNSQSTIAGISGNSITQDYCTAQKQVFGDTNTWEDHGGF
QSMTNAFKAGMVLVMSLWDDYYADMLWLDSVAYPTDADPSTPGVARGTCS
TTSGVPSDIESSAASAYVIYSNIKVGPINSTFSGT
3D structure
PDB4zzw Sequencing, Biochemical Characterization, Crystal Structure and Molecular Dynamics of Cellobiohydrolase Cel7A from Geotrichum Candidum 3C.
ChainA
Resolution1.5 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) E212 D214 E217 H228
Catalytic site (residue number reindexed from 1) E209 D211 E214 H225
Enzyme Commision number 3.2.1.-
3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end).
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 D343 R399 D340 R396
BS02 BGC A R251 D259 W380 R248 D256 W377
BS03 MG A D64 N206 D64 N203
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4zzw, PDBe:4zzw, PDBj:4zzw
PDBsum4zzw
PubMed26367132
UniProtA0A088T0J9

[Back to BioLiP]