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

6QFV

Human carbonic anhydrase II with bound IrCp* complex (cofactor 8) to generate an artificial transfer hydrogenase (ATHase)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002009biological_processmorphogenesis of an epithelium
A0004064molecular_functionarylesterase activity
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0015670biological_processcarbon dioxide transport
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0018820molecular_functioncyanamide hydratase activity
A0032230biological_processpositive regulation of synaptic transmission, GABAergic
A0032849biological_processpositive regulation of cellular pH reduction
A0038166biological_processangiotensin-activated signaling pathway
A0043209cellular_componentmyelin sheath
A0044070biological_processregulation of monoatomic anion transport
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0046903biological_processsecretion
A0051453biological_processregulation of intracellular pH
A0070050biological_processneuron cellular homeostasis
A0070062cellular_componentextracellular exosome
A2001150biological_processpositive regulation of dipeptide transmembrane transport
A2001225biological_processregulation of chloride transport
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue J0N A 301
ChainResidue
AILE91
ATHR199
ATRP208
AZN302
AHOH524
AGLN92
AHIS94
AHIS96
AHIS119
AVAL121
APHE130
ALEU197
ATHR198

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS94
AHIS96
AHIS119
AJ0N301

site_idAC3
Number of Residues2
Detailsbinding site for residue SO4 A 303
ChainResidue
AASP242
ATRP244

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 304
ChainResidue
APRO21
AILE22
ALYS24
AHOH405
AHOH532

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
ChainResidueDetails
AHIS64

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
ChainResidueDetails
AHIS94

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
ChainResidueDetails
AHIS96
AHIS119

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
ChainResidueDetails
ATHR198

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
ChainResidueDetails
ATYR7

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
ChainResidueDetails
AASN62
AASN67

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
ChainResidueDetails
AGLN92

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER165
ASER172

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
AHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS94metal ligand
AHIS96metal ligand
AGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS119metal ligand
ATHR198activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon