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1QHZ

NATIVE TETRAGONAL STRUCTURE OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS

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 Residues7
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AHOH548
AHOH568
AHOH577
AHOH579
AHOH587
AHOH717
AHOH726

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AGLU157
AASP243
AHOH531
AHOH640
AHOH681
AHOH686

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLY127
AASP166
AASN168
AASN169
AHOH512
AHOH557

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP120
AGLU124
AGLU124
AHOH454

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
AGLU139
AGLU228
AHOH416
AHOH436
AHOH566
AHOH584
AHOH626

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
AASN256
AHOH552
AHOH567
AHOH597
AHOH648

site_idACI
Number of Residues1
DetailsACID/BASE
ChainResidue
AGLU139

site_idNUC
Number of Residues1
DetailsNUCLEOPHILE
ChainResidue
AGLU228

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

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PDB entries from 2024-10-09

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