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9QUB

Cryo-EM structure of the human NHA2-Fab complex

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
CTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues418
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
BMET1-ARG86
ALEU134-PRO144
ALEU190-LEU200
AALA243-LEU270
AGLN325-ARG339
AALA374-ALA390
ACYS441-ALA461
AGLY510-VAL537
BLEU134-PRO144
BLEU190-LEU200
BALA243-LEU270
BGLN325-ARG339
BALA374-ALA390
BCYS441-ALA461
BGLY510-VAL537
AMET1-ARG86

site_idSWS_FT_FI2
Number of Residues34
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BVAL87-ILE104
AVAL87-ILE104

site_idSWS_FT_FI3
Number of Residues102
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
BTHR105-GLY113
AGLY228-TRP233
AGLY291-VAL300
AGLY358-GLY361
ASER412-THR417
ATHR474-TYR486
BILE162-LYS171
BGLY228-TRP233
BGLY291-VAL300
BGLY358-GLY361
BSER412-THR417
BTHR474-TYR486
ATHR105-GLY113
AILE162-LYS171

site_idSWS_FT_FI4
Number of Residues38
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BASN114-GLY133
AASN114-GLY133

site_idSWS_FT_FI5
Number of Residues32
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BSER145-VAL161
ASER145-VAL161

site_idSWS_FT_FI6
Number of Residues34
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BTRP172-GLY189
ATRP172-GLY189

site_idSWS_FT_FI7
Number of Residues52
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BLYS201-LEU227
ALYS201-LEU227

site_idSWS_FT_FI8
Number of Residues16
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BGLY234-GLY242
AGLY234-GLY242

site_idSWS_FT_FI9
Number of Residues38
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BLEU271-LEU290
ALEU271-LEU290

site_idSWS_FT_FI10
Number of Residues46
DetailsTRANSMEM: Helical; Name=8 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BPHE301-ILE324
APHE301-ILE324

site_idSWS_FT_FI11
Number of Residues34
DetailsTRANSMEM: Helical; Name=9 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BTHR340-PHE357
ATHR340-PHE357

site_idSWS_FT_FI12
Number of Residues22
DetailsTRANSMEM: Helical; Name=10 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BSER362-LEU373
ASER362-LEU373

site_idSWS_FT_FI13
Number of Residues40
DetailsTRANSMEM: Helical; Name=11 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BVAL391-ALA411
AVAL391-ALA411

site_idSWS_FT_FI14
Number of Residues44
DetailsTRANSMEM: Helical; Name=12 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BVAL418-VAL440
AVAL418-VAL440

site_idSWS_FT_FI15
Number of Residues22
DetailsTRANSMEM: Helical; Name=13 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BTHR462-ASP473
ATHR462-ASP473

site_idSWS_FT_FI16
Number of Residues44
DetailsTRANSMEM: Helical; Name=14 => ECO:0000250|UniProtKB:A0A6P3HVI0
ChainResidueDetails
BGLY487-ILE509
AGLY487-ILE509

site_idSWS_FT_FI17
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.12, ECO:0000312|PDB:7B4L
ChainResidueDetails
BVAL244
BGLY275
BASP278
BASP279
AVAL244
AGLY275
AASP278
AASP279

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER49
ASER49

237735

PDB entries from 2025-06-18

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