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4KC7

Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031222biological_processarabinan catabolic process
A0046558molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031222biological_processarabinan catabolic process
B0046558molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity
B0046872molecular_functionmetal ion binding
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005576cellular_componentextracellular region
C0005975biological_processcarbohydrate metabolic process
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0031222biological_processarabinan catabolic process
C0046558molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 501
ChainResidue
AHIS31
AHIS48
APHE116
ATYR341

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
AHOH940
AHOH942
AHIS314
AHOH929
AHOH930
AHOH931
AHOH932

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 501
ChainResidue
BHIS31
BHIS48
BTRP95
BPHE116
BTYR341

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG B 502
ChainResidue
BASN384
BGLU428
BVAL433
BTYR435
BSER458
BGLN460
BVAL462

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BHIS314
BHOH758
BHOH772
BHOH773
BHOH774

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG C 501
ChainResidue
CTYR148
CSER149
CGLY152

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 502
ChainResidue
CHIS314
CHOH774
CHOH776
CHOH796

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"24469445","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"24469445","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues33
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24469445","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsSite: {"description":"Important for substrate recognition","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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