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2D0D

Crystal Structure of a Meta-cleavage Product Hydrolase (CumD) A129V Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 400
ChainResidue
ASER34
ASER103
APHE104

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
AHOH639
AHOH655
AHOH689
AHOH769
AGLU215
AARG241
AGLN258
AARG261
AHOH556
AHOH621

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
AASP121
AARG122
AARG241
AHOH429
AHOH682
AHOH726

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1azw
ChainResidueDetails
ASER103
AASP224
AHIS252

site_idMCSA1
Number of Residues5
DetailsM-CSA 771
ChainResidueDetails
ASER34electrostatic stabiliser
ASER103nucleofuge, nucleophile, proton acceptor, proton donor
APHE104electrostatic stabiliser
AASP224electrostatic stabiliser
AHIS252proton acceptor, proton donor

242842

PDB entries from 2025-10-08

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