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5UAM

Structure of a new family of Polysaccharide lyase PL25-Ulvanlyase.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0005886cellular_componentplasma membrane
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 501
ChainResidue
ALYS359
AARG386

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
AHIS208
AHIS264
ACYS266
AHIS278

site_idAC3
Number of Residues10
Detailsbinding site for residue PO4 A 503
ChainResidue
AARG204
AHIS208
ATYR246
AEDO509
AHOH707
AHOH770
AHOH847
AHIS123
AHIS143
ATYR188

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
AASN299
AGLU301
ALYS317
ATRP371
AEDO510
AHOH822
AHOH978

site_idAC5
Number of Residues1
Detailsbinding site for residue K A 505
ChainResidue
AILE64

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 506
ChainResidue
ATHR280
APHE329
ATHR355
ALYS359
AHOH786
AHOH894

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 507
ChainResidue
AHIS208
AARG209
AHOH626
AHOH667

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO A 508
ChainResidue
AASP211
ALYS232
AHIS233
AHOH607
AHOH749
BGLY368

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO A 509
ChainResidue
AHIS143
AHIS158
AARG204
AALA207
AHIS208
APO4503
AHOH862

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO A 510
ChainResidue
AASP315
AGLU316
AMET319
AARG322
AGOL504
BARG169

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO A 511
ChainResidue
ATYR188
ATYR246
AARG282
APHE329
AHOH742
AHOH838
AHOH847

site_idAD3
Number of Residues3
Detailsbinding site for residue CL B 501
ChainResidue
BLYS359
BARG386
BHOH1049

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN B 502
ChainResidue
BHIS208
BHIS264
BCYS266
BHIS278

site_idAD5
Number of Residues9
Detailsbinding site for residue PO4 B 503
ChainResidue
BHIS123
BHIS143
BTYR188
BARG204
BHIS208
BTYR246
BEDO505
BHOH686
BHOH692

site_idAD6
Number of Residues1
Detailsbinding site for residue K B 504
ChainResidue
BILE64

site_idAD7
Number of Residues5
Detailsbinding site for residue EDO B 505
ChainResidue
BHIS143
BARG204
BALA207
BHIS208
BPO4503

site_idAD8
Number of Residues8
Detailsbinding site for residue EDO B 506
ChainResidue
BTHR280
BTHR328
BPHE329
BTHR355
BLYS359
BHOH680
BHOH761
BHOH903

site_idAD9
Number of Residues3
Detailsbinding site for residue EDO B 507
ChainResidue
BARG105
BGLY107
BHOH882

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:28290654
ChainResidueDetails
AHIS123
BHIS123

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:28290654
ChainResidueDetails
ATYR188
BTYR188

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:28290654
ChainResidueDetails
ACYS266
AHIS278
BASN60
BASN122
BLYS125
BHIS143
BARG204
BHIS208
BTYR246
BHIS264
BCYS266
BHIS278
AASN60
AASN122
ALYS125
AHIS143
AARG204
AHIS208
ATYR246
AHIS264

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Neutralizes the sugar carboxylate group at subsite +1 => ECO:0000305|PubMed:28290654
ChainResidueDetails
AARG204
BARG204

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PDB entries from 2024-05-29

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