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

1H2J

ENDOGLUCANASE CEL5A IN COMPLEX WITH UNHYDROLYSED AND COVALENTLY LINKED 2,4-DINITROPHENYL-2-DEOXY-2-FLUORO-CELLOBIOSIDE AT 1.15 A RESOLUTION

Replaces:  1HF7
Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1307
ChainResidue
AARG53
AHOH2377
AHOH2378

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE DCB A 1304
ChainResidue
ALEU103
AASN138
AGLU139
ATRP178
ATYR202
AGLU228
AALA234
ATHR235
AGLY236
ATRP262
ALYS267
AGLU269
AHOH2037
AHOH2368
AHOH2369
AHOH2370
AHOH2371
AHOH2372
AHOH2373
AGLU22
AARG23
AHIS35
ATRP39
ATYR66
AHIS101

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1305
ChainResidue
AGLU80
ALYS83
AGLU84
AGLU87
ALYS152
AGLU156
AGLN189
AHOH2135
AHOH2223
AHOH2260

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1306
ChainResidue
ASER13
AASN168
AGLY204
AALA233
AHOH2013
AHOH2015
AHOH2038
AHOH2374
AHOH2375
AHOH2376

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VIYEIANEPN
ChainResidueDetails
AVAL132-ASN141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:12595701, ECO:0000305|PubMed:9485319, ECO:0000305|PubMed:9718293, ECO:0000305|DOI:10.1021/ja984238n
ChainResidueDetails
AGLU139

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0000269|DOI:10.1021/ja984238n, ECO:0007744|PDB:1H11, ECO:0007744|PDB:1QI2, ECO:0007744|PDB:5A3H, ECO:0007744|PDB:6A3H, ECO:0007744|PDB:8A3H
ChainResidueDetails
AGLU228

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H
ChainResidueDetails
AHIS35

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0, ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H
ChainResidueDetails
ATRP39
ATYR66
ALYS267

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9718293, ECO:0000269|DOI:10.1021/ja984238n, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:3A3H
ChainResidueDetails
AHIS101

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:3A3H
ChainResidueDetails
ATYR202
AALA234

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0000269|DOI:10.1021/ja984238n, ECO:0007744|PDB:1H5V, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0, ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H, ECO:0007744|PDB:8A3H
ChainResidueDetails
ATRP262

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AASN138
AGLU228
AHIS200
AGLU139
ATYR202

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AGLU139

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon