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1MUM

Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
A0046421molecular_functionmethylisocitrate lyase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0016829molecular_functionlyase activity
B0016833molecular_functionoxo-acid-lyase activity
B0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
B0046421molecular_functionmethylisocitrate lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1001
ChainResidue
AASP58
AASP87
AHOH1006
AHOH1031
AHOH1044
AHOH1076
AHOH1093

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1002
ChainResidue
BHOH1047
BHOH1058
BHOH1125
BHOH1173
BASP58
BASP87

Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR
ChainResidueDetails
ALYS121-ARG126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538
ChainResidueDetails
AGLY46
BTHR159
BALA189
BILE211
BALA242
BASN271
AGLY124
ATHR159
AALA189
AILE211
AALA242
AASN271
BGLY46
BGLY124

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:12706720, ECO:0000269|PubMed:15723538
ChainResidueDetails
AALA86
AILE88
BALA86
BILE88

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 182
ChainResidueDetails
ALEU44proton acceptor, proton donor
AILE211electrostatic stabiliser, hydrogen bond donor
ALEU59hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AALA86metal ligand
AILE88metal ligand
AILE114proton acceptor, proton donor, proton relay
AASP116proton acceptor, proton donor, proton relay
AGLY124hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATHR159electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
AALA189electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

site_idMCSA2
Number of Residues10
DetailsM-CSA 182
ChainResidueDetails
BLEU44proton acceptor, proton donor
BILE211electrostatic stabiliser, hydrogen bond donor
BLEU59hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BALA86metal ligand
BILE88metal ligand
BILE114proton acceptor, proton donor, proton relay
BASP116proton acceptor, proton donor, proton relay
BGLY124hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BTHR159electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
BALA189electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

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건을2024-03-27부터공개중

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