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1MUC

STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION

Replaces:  1MLE
Functional Information from GO Data
ChainGOidnamespacecontents
A0006518biological_processpeptide metabolic process
A0009063biological_processamino acid catabolic process
A0016853molecular_functionisomerase activity
A0016854molecular_functionracemase and epimerase activity
A0018849molecular_functionmuconate cycloisomerase activity
A0018850molecular_functionchloromuconate cycloisomerase activity
A0030145molecular_functionmanganese ion binding
A0042952biological_processbeta-ketoadipate pathway
A0046872molecular_functionmetal ion binding
B0006518biological_processpeptide metabolic process
B0009063biological_processamino acid catabolic process
B0016853molecular_functionisomerase activity
B0016854molecular_functionracemase and epimerase activity
B0018849molecular_functionmuconate cycloisomerase activity
B0018850molecular_functionchloromuconate cycloisomerase activity
B0030145molecular_functionmanganese ion binding
B0042952biological_processbeta-ketoadipate pathway
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 374
ChainResidue
AASP198
AGLU224
AASP249
AHOH390
AHOH408
AHOH444

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 374
ChainResidue
BASP198
BGLU224
BASP249
BHOH390
BHOH412
BHOH451

site_idMNA
Number of Residues6
DetailsRESIDUES INVOLVED IN THE COORDINATION OF MN-ION IN CHAIN A.
ChainResidue
AASP198
AASP249
AGLU224
AHOH390
AHOH408
AHOH444

site_idMNB
Number of Residues6
DetailsRESIDUES INVOLVED IN THE COORDINATION OF MN-ION IN CHAIN .
ChainResidue
BHOH394
BHOH412
BHOH448
BASP198
BASP249
BGLU224

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AkSGIEsALlDAqGKrlglPVseLLG
ChainResidueDetails
AALA104-GLY129

site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. VrvDvNqywdesqAiracqvLgdngidlIEQP
ChainResidueDetails
AVAL195-PRO226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 7500361, 9724714, 10336378
ChainResidueDetails
ALYS169
ALYS167
AGLU327

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 7500361, 9724714, 10336378
ChainResidueDetails
BLYS169
BLYS167
BGLU327

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PDB entries from 2025-07-23

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