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

5Z87

Structural of a novel b-glucosidase EmGH1 at 2.3 angstrom from Erythrobacter marinus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0009044molecular_functionxylan 1,4-beta-xylosidase activity
A0045493biological_processxylan catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0009044molecular_functionxylan 1,4-beta-xylosidase activity
B0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue DTT A 801
ChainResidue
ATYR93
AGLU130
AARG192
ALYS233
AHIS234
AHIS281
AASP313
ATYR452
AGLU541

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 802
ChainResidue
ATHR538
AARG552
AARG583

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 803
ChainResidue
AASP713
AILE715
AHOH925
AHOH967
AHOH971
AHOH999

site_idAC4
Number of Residues2
Detailsbinding site for residue MG A 804
ChainResidue
AASP292
AHOH1248

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 805
ChainResidue
ATYR639
AGOL815
AHOH923
AHOH955
AHOH963
AHOH1078
BHIS251

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 806
ChainResidue
AASP57
ATYR84
APRO356
AARG360
AHOH972
AHOH1003
AHOH1071

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 807
ChainResidue
AVAL619
AASN620
ALEU732
AHOH905

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 808
ChainResidue
AGLN677
AGLU679
AGLN742

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO A 809
ChainResidue
AARG266
AASP756
AGLY757

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 810
ChainResidue
AASP553
AHOH1183
BSER654
BPEG809

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO A 811
ChainResidue
ASER117
BSER117
BARG118
BBEN802

site_idAD3
Number of Residues6
Detailsbinding site for residue PEG A 812
ChainResidue
APRO201
AHIS202
AASN259
APRO263
APEG813
AHOH919

site_idAD4
Number of Residues11
Detailsbinding site for residue PEG A 813
ChainResidue
APRO201
AASN259
AVAL260
ATYR641
APRO721
AGLU724
AARG726
APEG812
APEG814
AHOH968
AHOH1171

site_idAD5
Number of Residues9
Detailsbinding site for residue PEG A 814
ChainResidue
AVAL255
ALYS643
AALA719
AARG720
APRO721
AGLU724
APEG813
BASP285
BGLY286

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL A 815
ChainResidue
AHIS251
AGOL805
AHOH1163
BTYR639
BHOH980
BHOH988
BHOH1005

site_idAD7
Number of Residues9
Detailsbinding site for residue DTT B 801
ChainResidue
BTYR93
BGLU130
BARG192
BLYS233
BHIS234
BHIS281
BASP313
BTYR452
BGLU541

site_idAD8
Number of Residues13
Detailsbinding site for residue BEN B 802
ChainResidue
AGLY122
AEDO811
BVAL116
BSER117
BSER119
BARG120
BPHE121
BGLY122
AVAL116
ASER117
ASER119
AARG120
APHE121

site_idAD9
Number of Residues3
Detailsbinding site for residue MG B 803
ChainResidue
BTHR538
BARG552
BARG583

site_idAE1
Number of Residues6
Detailsbinding site for residue MG B 804
ChainResidue
BASP713
BILE715
BHOH948
BHOH1015
BHOH1022
BHOH1054

site_idAE2
Number of Residues6
Detailsbinding site for residue GOL B 805
ChainResidue
BASP57
BTYR84
BARG360
BHOH1075
BHOH1138
BHOH1168

site_idAE3
Number of Residues7
Detailsbinding site for residue GOL B 806
ChainResidue
BILE269
BGLY273
BSER274
BGLU307
BGLY308
BLYS382
BHOH1256

site_idAE4
Number of Residues4
Detailsbinding site for residue EDO B 807
ChainResidue
BVAL619
BASN620
BHOH938
BHOH1143

site_idAE5
Number of Residues4
Detailsbinding site for residue EDO B 808
ChainResidue
BLEU429
BGLN430
BTHR574
BHOH959

site_idAE6
Number of Residues7
Detailsbinding site for residue PEG B 809
ChainResidue
AASP553
AASP554
AEDO810
BLEU588
BASN632
BHOH1291
BHOH1399

site_idAE7
Number of Residues7
Detailsbinding site for residue PEG B 810
ChainResidue
BILE252
BPRO254
BMET257
BILE284
BASP292
BHIS294
BHOH1114

site_idAE8
Number of Residues9
Detailsbinding site for residue PEG B 811
ChainResidue
BASN259
BLYS643
BALA719
BARG720
BGLU724
BARG726
BTYR752
BHOH1239
BHOH1343

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pn.AAsVHLGGY
ChainResidueDetails
APRO442-TYR452

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon