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2HFW

Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0009617biological_processresponse to bacterium
A0016151molecular_functionnickel cation binding
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS94
AHIS96
AHIS119
AHOH326

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYaaELHLV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16042381, ECO:0000269|PubMed:17427958
ChainResidueDetails
AHIS94
AHIS96
AHIS119

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR199

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P07450
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
ASER29
ASER43
ASER48
ASER50
ASER55
ASER220

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
ATHR73
ATHR130
ATHR217

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
ATYR128

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P16015
ChainResidueDetails
ATHR177

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
ASER183
ASER188

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
AHIS64

224572

PDB entries from 2024-09-04

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