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1YM3

Crystal Structure of carbonic anhydrase RV3588c from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS51
AASP53
AHIS104
ACYS107

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AHIS199
AHOH303
AHOH305
AHOH307
AHOH315

Functional Information from PROSITE/UniProt
site_idPS00704
Number of Residues8
DetailsPROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CADSRVaA
ChainResidueDetails
ACYS51-ALA58

site_idPS00705
Number of Residues21
DetailsPROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. EYAVtvLnvplIVVlGHdsCG
ChainResidueDetails
AGLU88-GLY108

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15753099, ECO:0000269|PubMed:16321983, ECO:0007744|PDB:1YM3, ECO:0007744|PDB:2A5V
ChainResidueDetails
ACYS51
AHIS104
ACYS107

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15753099, ECO:0007744|PDB:1YM3
ChainResidueDetails
AASP53

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
AASP53
AARG55

219140

PDB entries from 2024-05-01

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