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2ZUM

Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A 459
ChainResidue
AGLU72
ATHR73
AHIS155
AARG156
ATRP377
AHOH556
AHOH712
AHOH831

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 460
ChainResidue
AGLU342
AHOH533
AHOH795
AHOH830
AGLU201

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ZN A 461
ChainResidue
AHIS76
AGLU108
AASP175
AZN463
AHOH562
AHOH586
AHOH833
AHOH839
AHOH840

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 462
ChainResidue
AASP321
AHIS325
AHOH832
AHOH835
AHOH838

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 463
ChainResidue
AGLU108
AASP175
AZN461
AHOH562
AHOH833

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 464
ChainResidue
AHIS62
AASP120
ASER122
AASP410
AHOH837

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 465
ChainResidue
ATHR47
AILE61
AHIS62
ATRP82
ACYS372
AASP373
AHOH841

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 466
ChainResidue
AHIS349
AASP400
AHOH716
AHOH836

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 467
ChainResidue
AHIS161
AGLU169
AHOH646
AHOH803
AHOH823
AHOH851
AHOH852

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 468
ChainResidue
AGOL469

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 469
ChainResidue
ALYS141
ATYR190
ATRP191
AGOL468

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 470
ChainResidue
ATYR33
AGOL475

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 471
ChainResidue
ALYS83
AHOH853

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 472
ChainResidue
ATRP272
ATRP273
AHOH495
AHOH795

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 473
ChainResidue
AASN85
AGLU87
AASP88
ALEU91
AHOH567
AHOH719
AHOH731

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 474
ChainResidue
ATYR49
AGLY80
ALEU81
ATRP82
ALYS83
ATRP394
AGOL476
AHOH484

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 475
ChainResidue
ATYR33
AGLN34
AGOL470

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 476
ChainResidue
ATYR49
AGLU58
AASN75
AHIS79
AASP382
AGOL474
AHOH484
AHOH595

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. IGADLKNEPH
ChainResidueDetails
AILE194-HIS203

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AGLU342
AGLU201
AASN200
AHIS297
ATYR299

223166

PDB entries from 2024-07-31

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