eF-site ID 1hp7-A PDB Code 1hp7 Chain A click to enlarge Title A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS Classification PROTEIN BINDING Compound ALPHA-1-ANTITRYPSIN Source Homo sapiens (Human) (A1AT_HUMAN) Sequence A:  DHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIA TAFAMLSLGTKGDTHDEILEGLNFNLTEIPEAQIHEGFQE LLHTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLY HSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDR DTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKV PMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEG KLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYD LKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVL TIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIDQN TKSPLFMGKVVNPTQK Description Functional site 1) chain A residue 73 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 2) chain A residue 89 type sequence E description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 3) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 4) chain A residue 151 type sequence E description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 5) chain A residue 175 type sequence E description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 6) chain A residue 231 type sequence H description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 7) chain A residue 256 type sequence D description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 8) chain A residue 43 type sequence H description BINDING SITE FOR RESIDUE ZN A 403 source : AC3 9) chain A residue 262 type sequence H description BINDING SITE FOR RESIDUE ZN A 403 source : AC3 10) chain A residue 285 type sequence S description BINDING SITE FOR RESIDUE ZN A 404 source : AC4 11) chain A residue 287 type sequence H description BINDING SITE FOR RESIDUE ZN A 404 source : AC4 12) chain A residue 324 type sequence E description BINDING SITE FOR RESIDUE ZN A 404 source : AC4 13) chain A residue 363 type sequence E description BINDING SITE FOR RESIDUE ZN A 404 source : AC4 14) chain A residue 98 type sequence E description BINDING SITE FOR RESIDUE ZN A 405 source : AC5 15) chain A residue 101 type sequence H description BINDING SITE FOR RESIDUE ZN A 405 source : AC5 16) chain A residue 139 type sequence H description BINDING SITE FOR RESIDUE ZN A 405 source : AC5 17) chain A residue 232 type sequence C description BINDING SITE FOR RESIDUE BME A 432 source : AC6 18) chain A residue 233 type sequence K description BINDING SITE FOR RESIDUE BME A 432 source : AC6 19) chain A residue 364-374 type prosite sequence VKFNKPFVFLM description SERPIN Serpins signature. VKFNKPFVFlM source prosite : PS00284 20) chain A residue 328 type SITE sequence K description (Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur => ECO:0000269|PubMed:3533918 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 330 type SITE sequence S description (Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases => ECO:0000269|PubMed:3533918 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 358 type SITE sequence M description Reactive bond source Swiss-Prot : SWS_FT_FI3 23) chain A residue 232 type MOD_RES sequence C description S-cysteinyl cysteine source Swiss-Prot : SWS_FT_FI5 24) chain A residue 359 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 46 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320 source Swiss-Prot : SWS_FT_FI7 26) chain A residue 83 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169 source Swiss-Prot : SWS_FT_FI8 27) chain A residue 247 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320 source Swiss-Prot : SWS_FT_FI9

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