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2V9L

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- E192A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005996biological_processmonosaccharide metabolic process
A0008994molecular_functionrhamnulose-1-phosphate aldolase activity
A0016829molecular_functionlyase activity
A0016830molecular_functioncarbon-carbon lyase activity
A0016832molecular_functionaldehyde-lyase activity
A0019299biological_processrhamnose metabolic process
A0019301biological_processrhamnose catabolic process
A0019323biological_processpentose catabolic process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A1275
ChainResidue
AHIS141
AHIS143
AHIS212
APO41276
APGO1283
AHOH2535

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A1276
ChainResidue
AASN32
AGLU117
AHIS141
AHIS143
AHIS212
AZN1275
APGO1283
AHOH2354
AHOH2535
AASN29
AGLY30
AGLY31

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A1277
ChainResidue
AASN29
ASER75
AGLY76
ATHR115
ASER116
AHOH2121
AHOH2348
AHOH2349
AHOH2536

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A1278
ChainResidue
ASER59
AGLY189
AASP191
AHOH2352
AHOH2538

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A1279
ChainResidue
ATYR102
APRO114
ATHR115
ASER116
ALEU118
AHOH2331
AHOH2539
AHOH2540

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACT A1280
ChainResidue
AGLY76
ALYS77
APHE78
AASP222
AHOH2306
AHOH2453
AHOH2541
AHOH2542
AHOH2543
AHOH2544
AHOH2545

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PGO A1281
ChainResidue
ATRP25
AGLU232
AGLN236
AHOH2097
AHOH2101
AHOH2460
AHOH2546
AHOH2547
AHOH2548

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO A1282
ChainResidue
AARG80
AGLN83
AHOH2043
AHOH2088
AHOH2549

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PGO A1283
ChainResidue
AHIS143
AGLU171
AHIS212
APHE263
AZN1275
APO41276
AHOH2120
AHOH2395
AHOH2396
AHOH2551

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGO A1284
ChainResidue
ALEU154
ATYR242
AMET244
ALYS248
AHOH2552
AHOH2553
AHOH2554

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGO A1285
ChainResidue
APRO57
ALEU58
ASER59
AGLN60
APRO61
AALA100
AHOH2555
AHOH2556

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO A1286
ChainResidue
ATHR250
AGLU255
AHOH2489
AHOH2558

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PGO A1287
ChainResidue
AHOH2428
AHOH2559
AHOH2560
AHOH2561
ATHR158
AGLU200
ALYS203
AHIS204
AHOH2405

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGO A1288
ChainResidue
AARG28
AVAL175
ASER217
AGLU223
ALEU227
AHOH2456
AHOH2562
AHOH2564

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479
ChainResidueDetails
AGLU117

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479
ChainResidueDetails
AHIS141
AHIS143
AHIS212

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gt7
ChainResidueDetails
AGLU117
AGLU171

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gt7
ChainResidueDetails
AVAL174

site_idMCSA1
Number of Residues5
DetailsM-CSA 645
ChainResidueDetails
AGLU117proton acceptor, proton donor
AHIS141metal ligand
AHIS143metal ligand
AGLU171proton donor
AHIS212metal ligand

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PDB entries from 2024-07-24

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