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4GWA

Crystal Structure of a GH7 Family Cellobiohydrolase from Limnoria quadripunctata

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016162molecular_functioncellulose 1,4-beta-cellobiosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016162molecular_functioncellulose 1,4-beta-cellobiosidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASP80
AHOH813
AHOH881
AHOH890
AHOH994
AHOH995

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AHOH752
AHOH832
AHOH983
AGLU139
AHOH697
AHOH733

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 503
ChainResidue
AHOH989
AHOH990
AHOH991
AHOH992
AHOH993

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BGLU139
BHOH744
BHOH944
BHOH945
BHOH946
BHOH947

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
AHOH974
AHOH980
BHOH959
BHOH960
BHOH961
BHOH1060

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 503
ChainResidue
AHOH986
BHOH954
BHOH955
BHOH956
BHOH957

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 504
ChainResidue
AGLU62
BHOH634
BHOH857
BHOH951
BHOH952
BHOH953
BHOH1092

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 505
ChainResidue
BHOH674
BHOH921
BHOH941
BHOH978
BHOH988
BHOH1090

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. GTVDSGSTLTVI
ChainResidueDetails
AGLY298-ILE309

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P62694
ChainResidueDetails
AGLU233
BGLU233

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P62694
ChainResidueDetails
AGLU238
BGLU238

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAQ
ChainResidueDetails
ATYR102
AASP124
ALYS202
BTYR102
BASP124
BLYS202

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAP, ECO:0007744|PDB:4IPM
ChainResidueDetails
AASP235
AHIS249
ATRP401
BASP235
BHIS249
BTRP401

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAQ, ECO:0007744|PDB:4IPM
ChainResidueDetails
AARG271
BARG271

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAP, ECO:0007744|PDB:4HAQ, ECO:0007744|PDB:4IPM
ChainResidueDetails
AASP279
AARG417
BASP279
BARG417

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PDB entries from 2024-10-30

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