Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2XHN

Rhamnogalacturonan lyase from Aspergillus aculeatus K150A active site mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0003824molecular_functioncatalytic activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016829molecular_functionlyase activity
A0016837molecular_functioncarbon-oxygen lyase activity, acting on polysaccharides
A0030246molecular_functioncarbohydrate binding
A0045490biological_processpectin catabolic process
A0071555biological_processcell wall organization
A0102210molecular_functionrhamnogalacturonan endolyase activity
B0000272biological_processpolysaccharide catabolic process
B0003824molecular_functioncatalytic activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016829molecular_functionlyase activity
B0016837molecular_functioncarbon-oxygen lyase activity, acting on polysaccharides
B0030246molecular_functioncarbohydrate binding
B0045490biological_processpectin catabolic process
B0071555biological_processcell wall organization
B0102210molecular_functionrhamnogalacturonan endolyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 800
ChainResidue
AGLU347
AASP349
AGLN351
AASP502
AHOH2761

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AGLY232
AHOH2067
AHOH2571
AHOH2941
AHOH2942
AHOH2943
AHOH2945
AASN19
ASER229
AARG230
ASER231

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
ALYS395
ALYS395
ASER490
ASER490
AHOH2946
AHOH2947
AHOH2948

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 903
ChainResidue
AARG429
AGLY488
AHOH2949
AHOH2951
AHOH2952

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 904
ChainResidue
ASER53
AARG107
AARG111
AHOH2537
AHOH2954

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1509
ChainResidue
ASER369
ASER369
AHOH2775
AHOH2777
AHOH2955
AHOH2955
AHOH2956

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 801
ChainResidue
BGLU347
BASP349
BGLN351
BASP502
BHOH2725

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 905
ChainResidue
BASN19
BSER229
BARG230
BSER231
BGLY232
BHOH2059
BHOH2528
BHOH2534
BHOH2920
BHOH2922

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 906
ChainResidue
BLYS395
BLYS395
BSER490
BSER490
BHOH2780
BHOH2780
BHOH2781
BHOH2781

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 907
ChainResidue
BARG429
BGLY488
BHOH2923

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 908
ChainResidue
BGLN47
BSER53
BARG107
BARG111
BHOH2496
BHOH2926
BHOH2927

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN331
BASN331

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon