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4GGB

Crystal structure of a proposed galactarolactone cycloisomerase from agrobacterium tumefaciens, TARGET EFI-500704, WITH BOUND CA, DISORDERED LOOPS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016836molecular_functionhydro-lyase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP194
AGLU220
AGLU246
AHOH567
AHOH678

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AHOH533
AHOH535
AGLU154
AGLU158
AASP368
ALEU370

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP209
AGLY237
AHOH668
AHOH669
AHOH675
AHOH676

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
AGLY250
ATYR252
AGLY253

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 405
ChainResidue
AVAL43
ATRP45
AARG367
AHOH633

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL A 406
ChainResidue
AGLN90
AGLN90
AGLY92
AGLY92
ALEU93
ALEU93
AHOH616
AHOH616

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 407
ChainResidue
AILE304
AASP331
AASN335
AARG338

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 408
ChainResidue
AALA115
ASER116
AMET119

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AlSGIDiALwDIkGKhygaSIsmLLG
ChainResidueDetails
AALA97-GLY122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS296

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASP194
AGLU220
AGLU246

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Increases basicity of active site His => ECO:0000250
ChainResidueDetails
AASP269

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 483
ChainResidueDetails
ALYS166proton shuttle (general acid/base)
AASP194metal ligand
AGLU220metal ligand
AGLU246metal ligand
AASP269modifies pKa
AHIS296proton shuttle (general acid/base)
AGLU329proton shuttle (general acid/base)

220113

PDB entries from 2024-05-22

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